Difference between revisions of "Phosphatase Subfamily PTPRK"

From PhosphataseWiki
Jump to: navigation, search
(→‎References)
(→‎Domain Structure)
 
(83 intermediate revisions by 2 users not shown)
Line 1: Line 1:
 
__NOTOC__
 
__NOTOC__
−
 
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:[[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPRK|Subfamily PTPRK]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:[[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPRK|Subfamily PTPRK]]
  
−
PTPRG is a receptor PTP family involved in metazoan neural development and maybe cancer.
+
PTPRK is a chordate-specific subfamily that regulates cell-cell adhesion. It is involved in human cancer and in the nervous system.  
  
 
===Evolution===
 
===Evolution===
−
PTPRK subfamily is vertebrate specific. There are four copies in human.
+
PTPRK is found in chordates (see [[Phosphatase_Subfamily_PPPRK_TN|technical notes]]). There are four copies in human, which have similar genomic organization, despite great disparities in gene size due to variations in intron length <cite>Besco04</cite>. PTPRK may be orthologous to some invertebrate phosphatases, including the [[Phosphatase_Subfamily_Ptp36E|Ptp36E]] subfamily
  
 
===Domain Structure===
 
===Domain Structure===
−
PTPRK has dual intracellular catalytic domains. The canonical extracellular domain combination is a MAM domain, Ig domain and multiple FN3 domain.  
+
PTPRK have dual intracellular catalytic domains and an extracellular region consisting of a MAM domain, 1 Ig domain and 4 FN3 domains <cite>Zondag95, Crossland96, Gebbink91</cite>. The MAM domain is essential for homophilic cell-cell interaction and helps determine the specificity of these interactions. Truncated PTPRM is properly expressed at the cell surface but fails to promote cell-cell adhesion. Homophilic cell adhesion is fully restored in a chimeric PTPRM molecule containing the MAM domain of PTPRK. However, this chimeric protein does not interact with either PTPRK or PTPRM <cite>Zondag95</cite>. The Ig domain of PTPRM contains the homophilic binding site and regulates subcellular localization <cite>Vecchio05</cite>.
−
 
+
−
MAM domain is essential for homophilic cell-cell interaction and helps determine the specificity of these interactions. Truncated PTPRM is properly expressed at the cell surface but fails to promote cell-cell adhesion. Homophilic cell adhesion is fully restored in a chimeric PTPRM molecule containing the MAM domain of PTPRK. However, this chimeric RPTP mu does not interact with either PTPRK or PTPRM <cite>Zondag95</cite>.  
+
  
 
===Functions===
 
===Functions===
−
PTPRK and PTPRM mediates homophilic cell-cell interaction <cite>Sap94, Zondag95</cite>.
+
PTPRK members mediate homophilic cell-cell interaction <cite>Sap94, Zondag95, Wang96, Brady93, McAndrew98a</cite>. They are putative tumor suppressors in various types of cancer. They also function in the nervous system.  
  
−
===== PTPRK =====
+
==== Human PTPRKs ====
−
Putative tumor suppressor <cite>Zhang98</cite>.
+
===== PTPRK (R-PTP-kappa) =====
 +
PTPRK is a putative tumor suppressor <cite>Zhang98</cite> in various types of cancer, such as breast cancer <cite>Sun13b</cite>, prostate cancer <cite>Sun13</cite>, lymphoma <cite>Flavell08</cite> and glioma <cite>Agarwal13</cite>. It plays its function as tumor suppressor through different mechanisms.
 +
PTPRK influences transactivating activity of beta-catenin in non-tumoral and neoplastic cells by regulating the balance between signaling and adhesive beta-catenin which is a molecule endowed with a dual function being involved both in cell adhesion and in Wnt signaling pathway <cite>Novellino08</cite>.
 +
PTPRK is a key factor in coordinating apoptosis via the regulation of MAPK pathways, in particular the JNK pathway in prostate cancer cells <cite>Sun13</cite>.
 +
PTPRK dephosphorylates Epidermal growth factor receptor (EGFR) and thereby regulates EGFR tyrosine phosphorylation and subsequent promotes human keratinocyte survival and proliferation <cite>Xu05</cite>. It is worthy pointing out that PTPRK is the target of transforming growth factor {beta} (TGF-{beta})-Smad, which inhibits proliferation and promotes cell migration <cite>Yang96, Wang05, Flavell08</cite>. PTPRK also dephosphorylates Src <cite>Wang05</cite>.
 +
 
 +
PTPRK regulates CD4+ T cell development through ERK1/2-mediated signaling <cite>Erdenebayar09</cite>.
 +
 
 +
===== PTPRM (PTP mu)=====
 +
PTPRM mediates homophilic cell-cell adhesion <cite>Brady93, Brady94, Gebbink93, Zondag95</cite>. It associates with and dephosphorylates cadherin and catenin <cite>Brady95, Brady98, Zondag00</cite>.
 +
It also binds and recruits the scaffolding protein RACK1, a scaffolding protein, to cell-cell contacts <cite>Brady01, Brady02</cite>.
 +
 
 +
PTPRM functions in developing nervous system. In particular, by interacting with E-cadherin, it regulates retinal ganglion cells neurite outgrowth and  the lamination of the retina by Brady-Kalnay's group <cite>Brady03, Brady04, Brady07</cite>. In addition, two other proteins have been reported to interact with PTPRM by Brady-Kalnay's group: i) IQGAP1, a known regulator of the Rho GTPases, Cdc42 and Rac1 <cite>Brady06</cite>, and ii) BRCA2 and CDKN1A interacting protein (BCCIP), a gene involved in cell cycle arrest and DNA repair <cite>Brady08</cite>.
 +
 
 +
PTPRM is involved in tumorigenesis and metastasis. It is proteolytically cleaved in glioblastoma multiforme (GBM), which yields PTPRM fragments that promote dispersal of GBM cells <cite>Kaur12</cite>; In breast cancer, it was observed that  decreased expression of PTPRM was correlated with poor prognosis and inversely correlated with disease free survival, and knockdown of PTPRM increased proliferation, adhesion, invasion and migration of breast cancer cells <cite>Sun12</cite>.
 +
 
 +
PTPRM is also expressed in specific [http://en.wikipedia.org/wiki/Endothelium vascular endothelial bed] <cite>Koop05, Bianchi99</cite>.
 +
 
 +
===== PTPRT (RPTPrho) =====
 +
PTPRT is restrictively expressed in the central nervous system and functions in regulating cadherin-mediated cell adhesion cellular adhesion in the central nervous system <cite>McAndrew98a, McAndrew98b, Besco06</cite>. In brain, PTPRT regulates synapse formation through interaction with cell adhesion molecules, and this function and the phosphatase activity are attenuated through tyrosine phosphorylation by the synaptic tyrosine kinase Fyn <cite>Lim09</cite>.
 +
 
 +
PTPRT is a putative tumor suppressor in colon cancer. PTPRT specifically dephosphorylated signal transducer and activator of transcription 3 (STAT3) at Y705 is essential for the function of STAT3 (Note: PTPRD dephosphorylate STAT3 Y705, as well). Overexpression of normal PTPRT in colorectal cancer cells reduced the expression of STAT3 target genes <cite>Zhang07</cite>. PTPRT knockout mice exhibit increased levels of colonic paxillin phosphorylation at residue Y88, which is found as a common feature of human colon cancers <cite>Zhao10</cite>.
 +
 
 +
PTPRT is the most frequently mutated PTP in different types of human cancers and is believed to be a tumor suppressor in colon cancer <cite>Scott11</cite> and head and neck squamous cell carcinoma <cite>Lui14</cite>, but it does not play a critical role in the development of common human cancers <cite>Lee07</cite>. It is worthy pointing out that more than half of the identified tumor-derived mutations are located in the extracellular part, particularly MAM domain and Ig domain, which mediates the homophilic interaction of cell-cell adhesion <cite>Yu08</cite>.
 +
 
 +
===== PTPRU (PTP-RO/hPTP-J/PTP pi/PTP lambda)=====
 +
PTPRU is predominantly expressed in adult brain, lung, and kidney <cite>Cheng97, Sommer97</cite>. It localizes to the adherens junctions with cell adhesion molecules like beta-catenin and E-cadherin <cite>Wang96</cite>. PTPRU directly binds and dephosphorylates beta-catenin, which is a key molecule involved in both cell adhesion and Wnt signaling pathway <cite>Yan02, Yan06</cite>. PTPRU-deficient mice exhibited hypertension and low [http://en.wikipedia.org/wiki/Glomerulus_%28kidney%29 glomerular] filtration rate <cite>Wharram00</cite>.
 +
 
 +
Weak PTPRU expression was detected in peripheral blood lymphocytes, thymus, and spleen even though gene expression was relatively high in the Jurkat T lymphoma cell line. Moreover, PTPRU gene expression was down-regulated after [http://en.wikipedia.org/wiki/Jurkat_cells Jurkat cells] (an immortalized line of human T lymphocyte cells) were stimulated by either Phorbol myristate acetage (PMA) or calcium ionophore <cite>Wang97, Wang99</cite>.
 +
 
 +
Both catalytic domains of PTPRU have substitutions that predict inactivity - the D1 domain has a D->E change in the WPD motif and a Y->E in the KNRY motif, while the D2 domain has E->A and F->S at these motifs. However, both domains have been reported to have in vitro catalytic activity <cite>Crossland96</cite>, and mutation of the catalytic cysteines in both domains blocks PTPRU ability to block beta catenin activation <cite>Yan06</cite>. 
 +
 
 +
=== External links ===
 +
OrthoDB links:
 +
* [http://cegg.unige.ch/orthodb5/results?level=Vertebrata&tree=Vert&searchtext=NCBI:5796 PTPRK]
 +
* [http://cegg.unige.ch/orthodb5/results?level=Vertebrata&tree=Vert&searchtext=NCBI:5797 PTPRM]
 +
* [http://cegg.unige.ch/orthodb5/results?level=Vertebrata&tree=Vert&searchtext=NCBI:11122 PTPRT]
 +
* [http://cegg.unige.ch/orthodb5/results?level=Vertebrata&tree=Vert&searchtext=NCBI:10076 PTPRU]
  
 
===References===
 
===References===
 
<biblio>
 
<biblio>
 +
#Besco06 pmid=16973135
 +
#Bianchi99 pmid=10094839
 +
#Brady94 pmid=7961788
 +
#Brady93 pmid=8394372
 +
#Brady95 pmid=7642713
 +
#Brady98 pmid=9531566
 +
#Brady01 pmid=11278757
 +
#Brady02 pmid=11801604
 +
#Brady03 pmid=14623235
 +
#Brady04 pmid=15080886
 +
#Brady06 pmid=16380380
 +
#Brady07 pmid=17276081
 +
#Brady08 pmid=18773424
 +
#Gebbink91 pmid=1655529
 +
#Gebbink93 pmid=8393854
 +
#Kaur12 pmid=22505657
 +
#Koop05 pmid=15706045
 +
#Lee07 pmid=17223850
 +
#Lim09 pmid=19816407
 +
#Lui14 pmid=24395800
 +
#McAndrew98a pmid=9602027
 +
#McAndrew98b pmid=9486824
 +
#Scott11 pmid=21517784
 +
#Sun12 pmid=23185569
 +
#Vecchio05 pmid=15491993
 +
#Wang99 pmid=10395944
 +
#Wharram00 pmid=11086029
 +
#Yu08 pmid=18644975
 +
#Zhang07 pmid=17360477
 +
#Zhao10 pmid=20133777
 +
#Zondag00 pmid=10753936
 +
 +
#Besco04 pmid=15040814
 
#Sap94 pmid=8264577
 
#Sap94 pmid=8264577
 
#Zondag95 pmid=7782276
 
#Zondag95 pmid=7782276
 +
#Wang96 pmid=8700514
 +
#Crossland96 pmid=8870675
 
#Zhang98 pmid=9722959
 
#Zhang98 pmid=9722959
 +
#Novellino08 pmid=16263724
 +
#Sun13 pmid=24002526
 +
#Sun13b pmid=23552869
 +
#Agarwa13 pmid=23696788
 +
#Flavell08 pmid=17720884
 +
#Kim11 pmid=21094132
 +
#Xu05 pmid=16263724
 +
#Wang05 pmid=15899872
 +
#Yang96 pmid=8941358
 +
#Erdenebayar09 pmid=19800317
 +
#Wang97 pmid=9070223
 +
#Cheng97 pmid=9054423
 +
#Sommer97 pmid=8989520
 +
#Yan02 pmid=12501215
 +
#Yan06 pmid=16574648
 
</biblio>
 
</biblio>

Latest revision as of 02:30, 10 November 2016

Phosphatase Classification: Fold CC1:Superfamily CC1: Family PTP: Subfamily PTPRK

PTPRK is a chordate-specific subfamily that regulates cell-cell adhesion. It is involved in human cancer and in the nervous system.

Evolution

PTPRK is found in chordates (see technical notes). There are four copies in human, which have similar genomic organization, despite great disparities in gene size due to variations in intron length [1]. PTPRK may be orthologous to some invertebrate phosphatases, including the Ptp36E subfamily

Domain Structure

PTPRK have dual intracellular catalytic domains and an extracellular region consisting of a MAM domain, 1 Ig domain and 4 FN3 domains [2, 3, 4]. The MAM domain is essential for homophilic cell-cell interaction and helps determine the specificity of these interactions. Truncated PTPRM is properly expressed at the cell surface but fails to promote cell-cell adhesion. Homophilic cell adhesion is fully restored in a chimeric PTPRM molecule containing the MAM domain of PTPRK. However, this chimeric protein does not interact with either PTPRK or PTPRM [2]. The Ig domain of PTPRM contains the homophilic binding site and regulates subcellular localization [5].

Functions

PTPRK members mediate homophilic cell-cell interaction [2, 6, 7, 8, 9]. They are putative tumor suppressors in various types of cancer. They also function in the nervous system.

Human PTPRKs

PTPRK (R-PTP-kappa)

PTPRK is a putative tumor suppressor [10] in various types of cancer, such as breast cancer [11], prostate cancer [12], lymphoma [13] and glioma [14]. It plays its function as tumor suppressor through different mechanisms. PTPRK influences transactivating activity of beta-catenin in non-tumoral and neoplastic cells by regulating the balance between signaling and adhesive beta-catenin which is a molecule endowed with a dual function being involved both in cell adhesion and in Wnt signaling pathway [15]. PTPRK is a key factor in coordinating apoptosis via the regulation of MAPK pathways, in particular the JNK pathway in prostate cancer cells [12]. PTPRK dephosphorylates Epidermal growth factor receptor (EGFR) and thereby regulates EGFR tyrosine phosphorylation and subsequent promotes human keratinocyte survival and proliferation [16]. It is worthy pointing out that PTPRK is the target of transforming growth factor {beta} (TGF-{beta})-Smad, which inhibits proliferation and promotes cell migration [13, 17, 18]. PTPRK also dephosphorylates Src [18].

PTPRK regulates CD4+ T cell development through ERK1/2-mediated signaling [19].

PTPRM (PTP mu)

PTPRM mediates homophilic cell-cell adhesion [2, 8, 20, 21]. It associates with and dephosphorylates cadherin and catenin [22, 23, 24]. It also binds and recruits the scaffolding protein RACK1, a scaffolding protein, to cell-cell contacts [25, 26].

PTPRM functions in developing nervous system. In particular, by interacting with E-cadherin, it regulates retinal ganglion cells neurite outgrowth and the lamination of the retina by Brady-Kalnay's group [27, 28, 29]. In addition, two other proteins have been reported to interact with PTPRM by Brady-Kalnay's group: i) IQGAP1, a known regulator of the Rho GTPases, Cdc42 and Rac1 [30], and ii) BRCA2 and CDKN1A interacting protein (BCCIP), a gene involved in cell cycle arrest and DNA repair [31].

PTPRM is involved in tumorigenesis and metastasis. It is proteolytically cleaved in glioblastoma multiforme (GBM), which yields PTPRM fragments that promote dispersal of GBM cells [32]; In breast cancer, it was observed that decreased expression of PTPRM was correlated with poor prognosis and inversely correlated with disease free survival, and knockdown of PTPRM increased proliferation, adhesion, invasion and migration of breast cancer cells [33].

PTPRM is also expressed in specific vascular endothelial bed [34, 35].

PTPRT (RPTPrho)

PTPRT is restrictively expressed in the central nervous system and functions in regulating cadherin-mediated cell adhesion cellular adhesion in the central nervous system [9, 36, 37]. In brain, PTPRT regulates synapse formation through interaction with cell adhesion molecules, and this function and the phosphatase activity are attenuated through tyrosine phosphorylation by the synaptic tyrosine kinase Fyn [38].

PTPRT is a putative tumor suppressor in colon cancer. PTPRT specifically dephosphorylated signal transducer and activator of transcription 3 (STAT3) at Y705 is essential for the function of STAT3 (Note: PTPRD dephosphorylate STAT3 Y705, as well). Overexpression of normal PTPRT in colorectal cancer cells reduced the expression of STAT3 target genes [39]. PTPRT knockout mice exhibit increased levels of colonic paxillin phosphorylation at residue Y88, which is found as a common feature of human colon cancers [40].

PTPRT is the most frequently mutated PTP in different types of human cancers and is believed to be a tumor suppressor in colon cancer [41] and head and neck squamous cell carcinoma [42], but it does not play a critical role in the development of common human cancers [43]. It is worthy pointing out that more than half of the identified tumor-derived mutations are located in the extracellular part, particularly MAM domain and Ig domain, which mediates the homophilic interaction of cell-cell adhesion [44].

PTPRU (PTP-RO/hPTP-J/PTP pi/PTP lambda)

PTPRU is predominantly expressed in adult brain, lung, and kidney [45, 46]. It localizes to the adherens junctions with cell adhesion molecules like beta-catenin and E-cadherin [7]. PTPRU directly binds and dephosphorylates beta-catenin, which is a key molecule involved in both cell adhesion and Wnt signaling pathway [47, 48]. PTPRU-deficient mice exhibited hypertension and low glomerular filtration rate [49].

Weak PTPRU expression was detected in peripheral blood lymphocytes, thymus, and spleen even though gene expression was relatively high in the Jurkat T lymphoma cell line. Moreover, PTPRU gene expression was down-regulated after Jurkat cells (an immortalized line of human T lymphocyte cells) were stimulated by either Phorbol myristate acetage (PMA) or calcium ionophore [50, 51].

Both catalytic domains of PTPRU have substitutions that predict inactivity - the D1 domain has a D->E change in the WPD motif and a Y->E in the KNRY motif, while the D2 domain has E->A and F->S at these motifs. However, both domains have been reported to have in vitro catalytic activity [3], and mutation of the catalytic cysteines in both domains blocks PTPRU ability to block beta catenin activation [48].

External links

OrthoDB links:

References

  1. Besco J, Popesco MC, Davuluri RV, Frostholm A, and Rotter A. Genomic structure and alternative splicing of murine R2B receptor protein tyrosine phosphatases (PTPkappa, mu, rho and PCP-2). BMC Genomics. 2004 Feb 11;5(1):14. DOI:10.1186/1471-2164-5-14 | PubMed ID:15040814 | HubMed [Besco04]
  2. Zondag GC, Koningstein GM, Jiang YP, Sap J, Moolenaar WH, and Gebbink MF. Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain. J Biol Chem. 1995 Jun 16;270(24):14247-50. DOI:10.1074/jbc.270.24.14247 | PubMed ID:7782276 | HubMed [Zondag95]
  3. Crossland S, Smith PD, and Crompton MR. Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase. Biochem J. 1996 Oct 1;319 ( Pt 1)(Pt 1):249-54. DOI:10.1042/bj3190249 | PubMed ID:8870675 | HubMed [Crossland96]
  4. Gebbink MF, van Etten I, Hateboer G, Suijkerbuijk R, Beijersbergen RL, Geurts van Kessel A, and Moolenaar WH. Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase. FEBS Lett. 1991 Sep 23;290(1-2):123-30. DOI:10.1016/0014-5793(91)81241-y | PubMed ID:1655529 | HubMed [Gebbink91]
  5. Del Vecchio RL and Tonks NK. The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase mu. J Biol Chem. 2005 Jan 14;280(2):1603-12. DOI:10.1074/jbc.M410181200 | PubMed ID:15491993 | HubMed [Vecchio05]
  6. Sap J, Jiang YP, Friedlander D, Grumet M, and Schlessinger J. Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding. Mol Cell Biol. 1994 Jan;14(1):1-9. DOI:10.1128/mcb.14.1.1-9.1994 | PubMed ID:8264577 | HubMed [Sap94]
  7. Wang H, Lian Z, Lerch MM, Chen Z, Xie W, and Ullrich A. Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family. Oncogene. 1996 Jun 20;12(12):2555-62. PubMed ID:8700514 | HubMed [Wang96]
  8. Brady-Kalnay SM, Flint AJ, and Tonks NK. Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. J Cell Biol. 1993 Aug;122(4):961-72. DOI:10.1083/jcb.122.4.961 | PubMed ID:8394372 | HubMed [Brady93]
  9. McAndrew PE, Frostholm A, White RA, Rotter A, and Burghes AH. Identification and characterization of RPTP rho, a novel RPTP mu/kappa-like receptor protein tyrosine phosphatase whose expression is restricted to the central nervous system. Brain Res Mol Brain Res. 1998 May;56(1-2):9-21. DOI:10.1016/s0169-328x(98)00014-x | PubMed ID:9602027 | HubMed [McAndrew98a]
  10. Zhang Y, Siebert R, Matthiesen P, Yang Y, Ha H, and Schlegelberger B. Cytogenetical assignment and physical mapping of the human R-PTP-kappa gene (PTPRK) to the putative tumor suppressor gene region 6q22.2-q22.3. Genomics. 1998 Jul 15;51(2):309-11. DOI:10.1006/geno.1998.5323 | PubMed ID:9722959 | HubMed [Zhang98]
  11. Sun PH, Ye L, Mason MD, and Jiang WG. Protein tyrosine phosphatase kappa (PTPRK) is a negative regulator of adhesion and invasion of breast cancer cells, and associates with poor prognosis of breast cancer. J Cancer Res Clin Oncol. 2013 Jul;139(7):1129-39. DOI:10.1007/s00432-013-1421-5 | PubMed ID:23552869 | HubMed [Sun13b]
  12. Sun PH, Ye L, Mason MD, and Jiang WG. Receptor-like protein tyrosine phosphatase κ negatively regulates the apoptosis of prostate cancer cells via the JNK pathway. Int J Oncol. 2013 Nov;43(5):1560-8. DOI:10.3892/ijo.2013.2082 | PubMed ID:24002526 | HubMed [Sun13]
  13. Flavell JR, Baumforth KR, Wood VH, Davies GL, Wei W, Reynolds GM, Morgan S, Boyce A, Kelly GL, Young LS, and Murray PG. Down-regulation of the TGF-beta target gene, PTPRK, by the Epstein-Barr virus encoded EBNA1 contributes to the growth and survival of Hodgkin lymphoma cells. Blood. 2008 Jan 1;111(1):292-301. DOI:10.1182/blood-2006-11-059881 | PubMed ID:17720884 | HubMed [Flavell08]
  14. Xu Y, Tan LJ, Grachtchouk V, Voorhees JJ, and Fisher GJ. Receptor-type protein-tyrosine phosphatase-kappa regulates epidermal growth factor receptor function. J Biol Chem. 2005 Dec 30;280(52):42694-700. DOI:10.1074/jbc.M507722200 | PubMed ID:16263724 | HubMed [Novellino08]
  15. Xu Y, Tan LJ, Grachtchouk V, Voorhees JJ, and Fisher GJ. Receptor-type protein-tyrosine phosphatase-kappa regulates epidermal growth factor receptor function. J Biol Chem. 2005 Dec 30;280(52):42694-700. DOI:10.1074/jbc.M507722200 | PubMed ID:16263724 | HubMed [Xu05]
  16. Yang Y, Gil M, Byun SM, Choi I, Pyun KH, and Ha H. Transforming growth factor-beta1 inhibits human keratinocyte proliferation by upregulation of a receptor-type tyrosine phosphatase R-PTP-kappa gene expression. Biochem Biophys Res Commun. 1996 Nov 21;228(3):807-12. DOI:10.1006/bbrc.1996.1736 | PubMed ID:8941358 | HubMed [Yang96]
  17. Wang SE, Wu FY, Shin I, Qu S, and Arteaga CL. Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function. Mol Cell Biol. 2005 Jun;25(11):4703-15. DOI:10.1128/MCB.25.11.4703-4715.2005 | PubMed ID:15899872 | HubMed [Wang05]
  18. Erdenebayar N, Maekawa Y, Nishida J, Kitamura A, and Yasutomo K. Protein-tyrosine phosphatase-kappa regulates CD4+ T cell development through ERK1/2-mediated signaling. Biochem Biophys Res Commun. 2009 Dec 18;390(3):489-93. DOI:10.1016/j.bbrc.2009.09.117 | PubMed ID:19800317 | HubMed [Erdenebayar09]
  19. Brady-Kalnay SM and Tonks NK. Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu. J Biol Chem. 1994 Nov 11;269(45):28472-7. PubMed ID:7961788 | HubMed [Brady94]
  20. Gebbink MF, Zondag GC, Wubbolts RW, Beijersbergen RL, van Etten I, and Moolenaar WH. Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase. J Biol Chem. 1993 Aug 5;268(22):16101-4. PubMed ID:8393854 | HubMed [Gebbink93]
  21. Brady-Kalnay SM, Rimm DL, and Tonks NK. Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo. J Cell Biol. 1995 Aug;130(4):977-86. DOI:10.1083/jcb.130.4.977 | PubMed ID:7642713 | HubMed [Brady95]
  22. Brady-Kalnay SM, Mourton T, Nixon JP, Pietz GE, Kinch M, Chen H, Brackenbury R, Rimm DL, Del Vecchio RL, and Tonks NK. Dynamic interaction of PTPmu with multiple cadherins in vivo. J Cell Biol. 1998 Apr 6;141(1):287-96. DOI:10.1083/jcb.141.1.287 | PubMed ID:9531566 | HubMed [Brady98]
  23. Zondag GC, Reynolds AB, and Moolenaar WH. Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn). J Biol Chem. 2000 Apr 14;275(15):11264-9. DOI:10.1074/jbc.275.15.11264 | PubMed ID:10753936 | HubMed [Zondag00]
  24. Mourton T, Hellberg CB, Burden-Gulley SM, Hinman J, Rhee A, and Brady-Kalnay SM. The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts. J Biol Chem. 2001 May 4;276(18):14896-901. DOI:10.1074/jbc.M010823200 | PubMed ID:11278757 | HubMed [Brady01]
  25. Hellberg CB, Burden-Gulley SM, Pietz GE, and Brady-Kalnay SM. Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells. J Biol Chem. 2002 Mar 29;277(13):11165-73. DOI:10.1074/jbc.M112157200 | PubMed ID:11801604 | HubMed [Brady02]
  26. Ensslen SE, Rosdahl JA, and Brady-Kalnay SM. The receptor protein tyrosine phosphatase mu, PTPmu, regulates histogenesis of the chick retina. Dev Biol. 2003 Dec 1;264(1):106-18. DOI:10.1016/j.ydbio.2003.08.009 | PubMed ID:14623235 | HubMed [Brady03]
  27. Ensslen SE and Brady-Kalnay SM. PTPmu signaling via PKCdelta is instructive for retinal ganglion cell guidance. Mol Cell Neurosci. 2004 Apr;25(4):558-71. DOI:10.1016/j.mcn.2003.12.003 | PubMed ID:15080886 | HubMed [Brady04]
  28. Oblander SA, Ensslen-Craig SE, Longo FM, and Brady-Kalnay SM. E-cadherin promotes retinal ganglion cell neurite outgrowth in a protein tyrosine phosphatase-mu-dependent manner. Mol Cell Neurosci. 2007 Mar;34(3):481-92. DOI:10.1016/j.mcn.2006.12.002 | PubMed ID:17276081 | HubMed [Brady07]
  29. Phillips-Mason PJ, Gates TJ, Major DL, Sacks DB, and Brady-Kalnay SM. The receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1. J Biol Chem. 2006 Feb 24;281(8):4903-10. DOI:10.1074/jbc.M506414200 | PubMed ID:16380380 | HubMed [Brady06]
  30. Phillips-Mason PJ, Mourton T, Major DL, and Brady-Kalnay SM. BCCIP associates with the receptor protein tyrosine phosphatase PTPmu. J Cell Biochem. 2008 Nov 1;105(4):1059-72. DOI:10.1002/jcb.21907 | PubMed ID:18773424 | HubMed [Brady08]
  31. Kaur H, Burden-Gulley SM, Phillips-Mason PJ, Basilion JP, Sloan AE, and Brady-Kalnay SM. Protein tyrosine phosphatase mu regulates glioblastoma cell growth and survival in vivo. Neuro Oncol. 2012 May;14(5):561-73. DOI:10.1093/neuonc/nos066 | PubMed ID:22505657 | HubMed [Kaur12]
  32. Sun PH, Ye L, Mason MD, and Jiang WG. Protein tyrosine phosphatase µ (PTP µ or PTPRM), a negative regulator of proliferation and invasion of breast cancer cells, is associated with disease prognosis. PLoS One. 2012;7(11):e50183. DOI:10.1371/journal.pone.0050183 | PubMed ID:23185569 | HubMed [Sun12]
  33. Koop EA, Gebbink MF, Sweeney TE, Mathy MJ, Heijnen HF, Spaan JA, Voest EE, VanBavel E, and Peters SL. Impaired flow-induced dilation in mesenteric resistance arteries from receptor protein tyrosine phosphatase-mu-deficient mice. Am J Physiol Heart Circ Physiol. 2005 Mar;288(3):H1218-23. DOI:10.1152/ajpheart.00512.2004 | PubMed ID:15706045 | HubMed [Koop05]
  34. Bianchi C, Sellke FW, Del Vecchio RL, Tonks NK, and Neel BG. Receptor-type protein-tyrosine phosphatase mu is expressed in specific vascular endothelial beds in vivo. Exp Cell Res. 1999 Apr 10;248(1):329-38. DOI:10.1006/excr.1999.4428 | PubMed ID:10094839 | HubMed [Bianchi99]
  35. McAndrew PE, Frostholm A, Evans JE, Zdilar D, Goldowitz D, Chiu IM, Burghes AH, and Rotter A. Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic fibroblast growth factor (FGF-1) transcripts delineate a rostrocaudal boundary in the granule cell layer of the murine cerebellar cortex. J Comp Neurol. 1998 Feb 22;391(4):444-55. DOI:10.1002/(sici)1096-9861(19980222)391:4<444::aid-cne3>3.0.co;2-0 | PubMed ID:9486824 | HubMed [McAndrew98b]
  36. Besco JA, Hooft van Huijsduijnen R, Frostholm A, and Rotter A. Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT). Brain Res. 2006 Oct 20;1116(1):50-7. DOI:10.1016/j.brainres.2006.07.122 | PubMed ID:16973135 | HubMed [Besco06]
  37. Lim SH, Kwon SK, Lee MK, Moon J, Jeong DG, Park E, Kim SJ, Park BC, Lee SC, Ryu SE, Yu DY, Chung BH, Kim E, Myung PK, and Lee JR. Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn. EMBO J. 2009 Nov 18;28(22):3564-78. DOI:10.1038/emboj.2009.289 | PubMed ID:19816407 | HubMed [Lim09]
  38. Zhang X, Guo A, Yu J, Possemato A, Chen Y, Zheng W, Polakiewicz RD, Kinzler KW, Vogelstein B, Velculescu VE, and Wang ZJ. Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T. Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):4060-4. DOI:10.1073/pnas.0611665104 | PubMed ID:17360477 | HubMed [Zhang07]
  39. Zhao Y, Zhang X, Guda K, Lawrence E, Sun Q, Watanabe T, Iwakura Y, Asano M, Wei L, Yang Z, Zheng W, Dawson D, Willis J, Markowitz SD, Satake M, and Wang Z. Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T. Proc Natl Acad Sci U S A. 2010 Feb 9;107(6):2592-7. DOI:10.1073/pnas.0914884107 | PubMed ID:20133777 | HubMed [Zhao10]
  40. Scott A and Wang Z. Tumour suppressor function of protein tyrosine phosphatase receptor-T. Biosci Rep. 2011 Oct;31(5):303-7. DOI:10.1042/BSR20100134 | PubMed ID:21517784 | HubMed [Scott11]
  41. Lui VW, Peyser ND, Ng PK, Hritz J, Zeng Y, Lu Y, Li H, Wang L, Gilbert BR, General IJ, Bahar I, Ju Z, Wang Z, Pendleton KP, Xiao X, Du Y, Vries JK, Hammerman PS, Garraway LA, Mills GB, Johnson DE, and Grandis JR. Frequent mutation of receptor protein tyrosine phosphatases provides a mechanism for STAT3 hyperactivation in head and neck cancer. Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):1114-9. DOI:10.1073/pnas.1319551111 | PubMed ID:24395800 | HubMed [Lui14]
  42. Lee JW, Jeong EG, Lee SH, Nam SW, Kim SH, Lee JY, Yoo NJ, and Lee SH. Mutational analysis of PTPRT phosphatase domains in common human cancers. APMIS. 2007 Jan;115(1):47-51. DOI:10.1111/j.1600-0463.2007.apm_554.x | PubMed ID:17223850 | HubMed [Lee07]
  43. Yu J, Becka S, Zhang P, Zhang X, Brady-Kalnay SM, and Wang Z. Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion. Mol Cancer Res. 2008 Jul;6(7):1106-13. DOI:10.1158/1541-7786.MCR-07-2123 | PubMed ID:18644975 | HubMed [Yu08]
  44. Cheng J, Wu K, Armanini M, O'Rourke N, Dowbenko D, and Lasky LA. A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors. J Biol Chem. 1997 Mar 14;272(11):7264-77. DOI:10.1074/jbc.272.11.7264 | PubMed ID:9054423 | HubMed [Cheng97]
  45. Sommer L, Rao M, and Anderson DJ. RPTP delta and the novel protein tyrosine phosphatase RPTP psi are expressed in restricted regions of the developing central nervous system. Dev Dyn. 1997 Jan;208(1):48-61. DOI:10.1002/(SICI)1097-0177(199701)208:1<48::AID-AJA5>3.0.CO;2-1 | PubMed ID:8989520 | HubMed [Sommer97]
  46. Yan HX, He YQ, Dong H, Zhang P, Zeng JZ, Cao HF, Wu MC, and Wang HY. Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin. Biochemistry. 2002 Dec 31;41(52):15854-60. DOI:10.1021/bi026095u | PubMed ID:12501215 | HubMed [Yan02]
  47. Yan HX, Yang W, Zhang R, Chen L, Tang L, Zhai B, Liu SQ, Cao HF, Man XB, Wu HP, Wu MC, and Wang HY. Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and increases E-cadherin-dependent cell adhesion. J Biol Chem. 2006 Jun 2;281(22):15423-33. DOI:10.1074/jbc.M602607200 | PubMed ID:16574648 | HubMed [Yan06]
  48. Wharram BL, Goyal M, Gillespie PJ, Wiggins JE, Kershaw DB, Holzman LB, Dysko RC, Saunders TL, Samuelson LC, and Wiggins RC. Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate. J Clin Invest. 2000 Nov;106(10):1281-90. DOI:10.1172/JCI7236 | PubMed ID:11086029 | HubMed [Wharram00]
  49. Wang B, Kishihara K, Zhang D, Hara H, and Nomoto K. Molecular cloning and characterization of a novel human receptor protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene expression by PMA and calcium ionophore in Jurkat T lymphoma cells. Biochem Biophys Res Commun. 1997 Feb 3;231(1):77-81. DOI:10.1006/bbrc.1997.6004 | PubMed ID:9070223 | HubMed [Wang97]
  50. Wang B, Kishihara K, Zhang D, Sakamoto T, and Nomoto K. Transcriptional regulation of a receptor protein tyrosine phosphatase gene hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T lymphoma cells. Biochim Biophys Acta. 1999 Jul 8;1450(3):331-40. DOI:10.1016/s0167-4889(99)00064-6 | PubMed ID:10395944 | HubMed [Wang99]
  51. Agarwal S, Al-Keilani MS, Alqudah MA, Sibenaller ZA, Ryken TC, and Assem M. Tumor derived mutations of protein tyrosine phosphatase receptor type k affect its function and alter sensitivity to chemotherapeutics in glioma. PLoS One. 2013;8(5):e62852. DOI:10.1371/journal.pone.0062852 | PubMed ID:23696788 | HubMed [Agarwa13]
  52. Kim YS, Jung JA, Kim HJ, Ahn YH, Yoo JS, Oh S, Cho C, Yoo HS, and Ko JH. Galectin-3 binding protein promotes cell motility in colon cancer by stimulating the shedding of protein tyrosine phosphatase kappa by proprotein convertase 5. Biochem Biophys Res Commun. 2011 Jan 7;404(1):96-102. DOI:10.1016/j.bbrc.2010.11.071 | PubMed ID:21094132 | HubMed [Kim11]
All Medline abstracts: PubMed | HubMed
Retrieved from "http://phosphatome.net/wiki/index.php?title=Phosphatase_Subfamily_PTPRK&oldid=3939"