Phosphatase Subfamily PTPN13 - Revision history

Gerard: /* PTPN13 and cancer */

2017-03-23T20:29:38Z

‎PTPN13 and cancer

Gerard at 20:29, 23 March 2017

2017-03-23T20:29:06Z

Gerard at 03:00, 16 May 2016

2016-05-16T03:00:44Z

Gerard at 02:52, 16 May 2016

2016-05-16T02:52:38Z

Gerard at 02:50, 16 May 2016

2016-05-16T02:50:41Z

Gerard: /* Evolution */

2016-05-16T02:47:33Z

‎Evolution

Mark: /* References */

2015-09-22T05:16:47Z

‎References

Mark: /* Functions */

2015-09-22T05:16:30Z

‎Functions

Mark: /* References */

2015-09-22T05:15:55Z

‎References

Mark: /* Functions */

2015-09-22T05:15:22Z

‎Functions

← Older revision		Revision as of 20:29, 23 March 2017
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	PTPN13 mediates the activation of NF-kappaB and induces resistance of head and neck cancer to Fas-induced apoptosis <cite>Wieckowski07</cite>.		PTPN13 mediates the activation of NF-kappaB and induces resistance of head and neck cancer to Fas-induced apoptosis <cite>Wieckowski07</cite>.

−	PTP20 is expressed in a wide range of both normal and transformed cell lines <cite>Fodero-Tavoletti05</cite>. RNA-seq data from GTEx shows it is expressed at very low level. PTPN20 locates to the nucleus and the microtubule network, colocalizing with the microtubule-organizing centre and intracellular membrane compartments, including the endoplasmic reticulum and the Golgi apparatus. Stimulation of cells with epidermal growth factor, osmotic shock, pervanadate, or integrin ligation targeted PTPN20 to actin-rich structures that included membrane ruffles <cite>Fodero-Tavoletti05</cite>. Human PTPN20 exhibited catalytic activity towards tyrosyl phosphorylated substrates <cite>Fodero-Tavoletti05</cite>.

		+	PTP20 is expressed in a wide range of both normal and transformed cell lines <cite>Fodero-Tavoletti05</cite>. RNA-seq data from GTEx shows it is expressed at very low level. PTPN20 locates to the nucleus and the microtubule network, colocalizing with the microtubule-organizing centre and intracellular membrane compartments, including the endoplasmic reticulum and the Golgi apparatus. Stimulation of cells with epidermal growth factor, osmotic shock, pervanadate, or integrin ligation targeted PTPN20 to actin-rich structures that included membrane ruffles <cite>Fodero-Tavoletti05</cite>. Human PTPN20 exhibited catalytic activity towards tyrosyl phosphorylated substrates <cite>Fodero-Tavoletti05</cite>.

	===References===		===References===

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 ===Evolution===
-PTPN13 is found in holozoa, but lost in ecdysozoa (including nematodes and insects). It has a single member in human, PTPN13 (FAP-1/PTP1E/PTPL1/PTP-BAS).
+PTPN13 is found in holozoa, but lost in ecdysozoa (including nematodes and insects). It has two human members, PTPN13 (FAP-1/PTP1E/PTPL1/PTP-BAS) and PTPN20. PTPN20 emerged in sarcopterygii,which include the coelacanths, lungfish, and the tetrapods. PTPN20 duplicated soon after it's emergence, with both copies losing part of their sequence: One has N-terminal region pseudogenized, which resulted in FRMPD2B (pseudogene) and PTPN20 (protein-coding); another one has C-terminal region pseudogenized, which resulted in FRMPD2 (protein-coding) and PTPN20C (pseudogene).
 === Domain Structure ===
-PTPN13 has FERM domain, followed by five PDZ domains and a PTP phosphatase domain. The earliest form, in Monosiga, has 7 PDZ domains.
+PTPN13 typically has a FERM domain followed by five PDZ domains and a PTP phosphatase domain. The earliest form, in Monosiga, has 7 PDZ domains.
-FERM domain are usually found in proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain of PTPN13 can bind to phosphatidyl-inositol-4,5-bisphosphate (PtdIns(4,5)P2) and this binding is important for plasma membrane localization of PTPN13 <cite>Hagemann13</cite>.
+FERM domains are usually found in proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain of PTPN13 can bind to phosphatidyl-inositol-4,5-bisphosphate (PtdIns(4,5)P2) and this binding is important for plasma membrane localization of PTPN13 <cite>Hagemann13</cite>.
 The five PDZ domains mediates the interactions between PTPN13 and different proteins in a specific manner:
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 The phosphatase domain crystal structure has been solved <cite>Villa05</cite>.
 ===Functions===
@@ Line 70: / Line 73: @@
 PTPN13 interacts with other proteins with PDZ domains (see Domain section above).
 PTPN13 is regulated by:
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 PTPN13 mediates the activation of NF-kappaB and induces resistance of head and neck cancer to Fas-induced apoptosis <cite>Wieckowski07</cite>.
 ===References===
@@ Line 99: / Line 106: @@
 #Dromard07 pmid=17638892
 #Erdmann00 pmid=10951583
 #Freiss11 pmid=21235435
 #Ghiran08 pmid=18684861

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPN13|Subfamily PTPN13]] (FAP-1/PTP1E/PTPL1/PTP-BAS)
-PTPN13 is a non-receptor PTP with diverse functions in intercellular signaling. It has various substrates and interacting partners. PTPN13 has a FERM domain localizing it to plasma membrane, five PDZ domains interacting with different proteins, and a phosphatase domain.
+PTPN13 is a non-receptor PTP with diverse functions in intercellular signaling.
 ===Evolution===
-PTPN13 is found in holozoa, but lost in ecdysozoa (including nematodes and insects). In particular, choanoflagellate Monosiga has a PTP with similar domain combination as vertebrate PTPN13, containing FERM domain, seven (instead of five) PDZ domains, and phosphatase domain from N- to C- terminus. PTPN13 has a single member in human: PTPN13 (FAP-1/PTP1E/PTPL1/PTP-BAS).
+PTPN13 is found in holozoa, but lost in ecdysozoa (including nematodes and insects). It has a single member in human, PTPN13 (FAP-1/PTP1E/PTPL1/PTP-BAS).
-=== Domain ===
+=== Domain Structure ===
 PTPN13 has FERM domain, followed by five PDZ domains and a PTP phosphatase domain. The earliest form, in Monosiga, has 7 PDZ domains.
@@ Line 44: / Line 44: @@
 ** CR1 (complement component (3b/4b) receptor 1 (Knops blood group)) <cite>Ghiran08</cite>
-Phosphatase domain has crystal structure solved <cite>Villa05</cite>.
+The phosphatase domain crystal structure has been solved <cite>Villa05</cite>.
 ===Functions===
 PTPN13 is widely expressed in normal human tissues and partly overlaps with Fas expression <cite>Saras94, Maekawa94, Lee99</cite>. PTPN13 has several substrates:
-* [http://en.wikipedia.org/wiki/Fas_receptor Fas receptor] (FasR), PTPN13 is also named Fap-1 (Fas-associated phosphatase 1), which specifically modulates (negatively regulates) Fas but not TRAIL signaling through dephosphorylation of FasR, also known as apoptosis antigen 1 (APO-1), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). Fas receptor is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway. The dephosphorylation FasR by PTPN13 reduces FasR cell surface expression and activity. PTPN13 binds to FasR at the C-terminal 15 amino acids of FasR that are necessary and sufficient for the interaction <cite>Sato95, Li00, Ivanov03</cite>.
+* [http://en.wikipedia.org/wiki/Fas_receptor Fas receptor] (FasR/TNFRSF6), PTPN13 is also named Fap-1 (Fas-associated phosphatase 1), which negatively regulates Fas but not TRAIL apoptotic signaling through dephosphorylation of FasR. Dephosphorylation FasR by PTPN13 reduces FasR cell surface expression and activity. PTPN13 binds to FasR at the C-terminal 15 amino acids of FasR <cite>Sato95, Li00, Ivanov03</cite>.
-* Src kinase. PTPN13 inhibits Src through direct dephosphorylation of Tyr-419 in intact cells <cite>Glondu-Lassis10</cite>.
+* Src kinase. PTPN13 inhibits Src through direct dephosphorylation of Tyr-419 <cite>Glondu-Lassis10</cite>.
 * Her2/ErbB2. PTPN13 inhibits Her2 activity by dephosphorylating the signal domain of Her2 and plays a role in attenuating invasiveness and metastasis of Her2 overactive tumors <cite>Zhu08</cite>.
@@ Line 57: / Line 57: @@
 * [http://en.wikipedia.org/wiki/IRS1 IRS1 (insulin receptor substrate-1)]. PTPN13 specifically dephosphorylates IRS1 in vitro and in vivo. IRS1 plays a key role in transmitting signals from the insulin and insulin-like growth factor-1 (IGF-1) receptors to intracellular pathways PI3K / Akt and Erk MAP kinase pathways <cite>Dromard07</cite>.
-* [http://en.wikipedia.org/wiki/GSK3B Glycogen synthase kinase beta (GSK3beta)]. PTPN13 interacts with adenomatous polyposis coli (Apc) protein, which participates in a complex that includes GSK3beta and beta-catenin. PTPN13 decreases activity and tyrosine phosphorylation of GSK3beta. GSK3beta phosphorylates beta-catenin and facilitates beta-catenin ubiquitination and degradation by the proteasome. Thus, PTPN13 modulates beta-catenin, the increased activity of which correlates with leukemia stem cell expansion and disease progression in chronic myeloid leukemia (CML) <cite>Huang13</cite>.
+* [http://en.wikipedia.org/wiki/GSK3B Glycogen synthase kinase beta (GSK3beta)]. PTPN13 interacts with adenomatous polyposis coli (Apc) protein, which participates in a complex that includes GSK3beta and beta-catenin. PTPN13 decreases activity and tyrosine phosphorylation of GSK3beta. GSK3beta phosphorylates beta-catenin and facilitates beta-catenin ubiquitination and degradation by the proteasome <cite>Huang13</cite>.
 * p85beta, a regulatory subunit of [http://en.wikipedia.org/wiki/Phosphoinositide_3-kinase  Phosphoinositide 3-kinase (PI3K)]. PTPN13 dephosphorylates pTyr-655 of p85beta and stimulates p85beta binding to and degradation through F-box protein FBXL2 <cite>Kuchay13</cite>.
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 * [http://en.wikipedia.org/wiki/I%CE%BAB%CE%B1 IkappaBalpha (nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha)] is one member of a family of cellular proteins that function to inhibit the NF-kappaB transcription factor, as evidenced from in vitro dephosphorylation reaction and substrate trapping mutant experiments <cite>Nakai00</cite>.
-* ERK and MEK. PTPN13 attenuates MEK and ERk phosphorylation <cite>Hoover09</cite>, but no direct evidence supported MEK and ERK are PTPN13's physiological substrates.
+* ERK and MEK. PTPN13 attenuates MEK and ERK phosphorylation <cite>Hoover09</cite>, though they are not known to be direct substrates.
-* [http://en.wikipedia.org/wiki/EFNB1 EphrinB1], a type I membrane protein and a ligand of Eph-related receptor tyrosine kinases. PPTPN13 loss increases phosphorylated EphrinB1 <cite>Vermeer12</cite>, but no strong evidence supported EphrinB1 is PTPN13's physiological substrate.
+* [http://en.wikipedia.org/wiki/EFNB1 EphrinB1] a ligand of Eph receptor tyrosine kinases. PPTPN13 loss increased phosphorylated EphrinB1 <cite>Vermeer12</cite>, but is not known to be a substrate..
 PTPN13 interacts with other proteins with PDZ domains (see Domain section above).
@@ Line 81: / Line 81: @@
 ====== PTPN13 and cancer ======
-PTPN13 is implicated in cancer. The impact of PTPN13 on cancer is divided between its capacity to counteract the activity of oncogenic tyrosine kinases (as tumor suppressor), its inhibitory interaction with the death receptor, Fas (as oncogene) <cite>Freiss11</cite>. Furthermore, PTPN13 has a key role in the apoptotic process in human breast cancer cells independent of Fas but associated with an early inhibition of the insulin receptor substrate-1/phosphatidylinositol 3-kinase pathway <cite>Bompard02</cite>. Here are some (not all) examples:
+PTPN13 is implicated in cancer. The impact of PTPN13 on cancer is divided between its capacity to counteract the activity of oncogenic tyrosine kinases (as tumor suppressor), its inhibitory interaction with the death receptor, Fas (as oncogene) <cite>Freiss11</cite>. Furthermore, PTPN13 has a key role in the apoptotic process in human breast cancer cells independent of Fas but associated with an early inhibition of the insulin receptor substrate-1/phosphatidylinositol 3-kinase pathway <cite>Bompard02</cite>. Here are some examples:
 PTPN13 has proapoptotic functions and can suppress tumorigenesis. However, its tumor suppressor functions were frequently disrupted epigenetically in multiple lymphomas and carcinomas owing to the methylation of a bidirectional promoter. It is worthy pointing out the promoter is in common with MAPK10/JNK3, which also functions as proapototic gene and tumor suppressor <cite>Ying06</cite>.

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPN13|Subfamily PTPN13]] (FAP-1/PTP1E/PTPL1/PTP-BAS)
-PTPN13 is a non-receptor PTP with diverse functions. It has various substrates and interacting partners. PTPN13 has a FERM domain localizing it to plasma membrane, five PDZ domains interacting with different proteins, and a phosphatase domain.
+PTPN13 is a non-receptor PTP with diverse functions in intercellular signaling. It has various substrates and interacting partners. PTPN13 has a FERM domain localizing it to plasma membrane, five PDZ domains interacting with different proteins, and a phosphatase domain.
 ===Evolution===

@@ Line 1: / Line 1: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPN13|Subfamily PTPN13]] (FAP-1/PTP1E/PTPL1/PTP-BAS)
-PTPN13 is a cytosolic PTP that has diverse functions. It has various substrates and interacting partners. PTPN13 has a FERM domain localizing it to plasma membrane, five PDZ domains interacting with different proteins, and a phosphatase domain. PTPN13 probably emerged in holozoan, but lost in various metazoan lineages such as ecdysozoan. PTPN13 has a single member in human: PTPN13/FAP-1/PTP1E/PTPL1/PTP-BAS.
+PTPN13 is a non-receptor PTP with diverse functions. It has various substrates and interacting partners. PTPN13 has a FERM domain localizing it to plasma membrane, five PDZ domains interacting with different proteins, and a phosphatase domain.
 ===Evolution===
-PTPN13 is found in holozoa, but lost in ecdysozoa (including nematodes and insects). In particular, choanoflagellate Monosiga has a PTP with similar domain combination as vertebrate PTPN13, containing FERM domain, seven (instead of five) PDZ domains, and phosphatase domain from N- to C- terminus. Thus, PTPN13 probably emerged in holozoan, but lost in different lineages, such as ecdysozoan.
+PTPN13 is found in holozoa, but lost in ecdysozoa (including nematodes and insects). In particular, choanoflagellate Monosiga has a PTP with similar domain combination as vertebrate PTPN13, containing FERM domain, seven (instead of five) PDZ domains, and phosphatase domain from N- to C- terminus. PTPN13 has a single member in human: PTPN13 (FAP-1/PTP1E/PTPL1/PTP-BAS).
 === Domain ===
-PTPN13 has FERM domain, five PDZ domains, phosphatase domain in the order from N- to C- terminus.
+PTPN13 has FERM domain, followed by five PDZ domains and a PTP phosphatase domain. The earliest form, in Monosiga, has 7 PDZ domains.
-FERM domain are usually found in proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain of PTPN13 can bind to phosphatidyl-inositol-4,5-bisphosphate (PtdIns(4,5)P2) and this binding
+FERM domain are usually found in proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain of PTPN13 can bind to phosphatidyl-inositol-4,5-bisphosphate (PtdIns(4,5)P2) and this binding is important for plasma membrane localization of PTPN13 <cite>Hagemann13</cite>.
 is important for plasma membrane localization of PTPN13 <cite>Hagemann13</cite>.
 The five PDZ domains mediates the interactions between PTPN13 and different proteins in a specific manner:
@@ Line 47: / Line 47: @@
 ===Functions===
-PTPN13 is widely expressed in normal human tissues and partly overlapped with Fas expression <cite>Saras94, Maekawa94, Lee99</cite>. PTPN13 have below substrates:
+PTPN13 is widely expressed in normal human tissues and partly overlaps with Fas expression <cite>Saras94, Maekawa94, Lee99</cite>. PTPN13 has several substrates:
 * [http://en.wikipedia.org/wiki/Fas_receptor Fas receptor] (FasR), PTPN13 is also named Fap-1 (Fas-associated phosphatase 1), which specifically modulates (negatively regulates) Fas but not TRAIL signaling through dephosphorylation of FasR, also known as apoptosis antigen 1 (APO-1), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). Fas receptor is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway. The dephosphorylation FasR by PTPN13 reduces FasR cell surface expression and activity. PTPN13 binds to FasR at the C-terminal 15 amino acids of FasR that are necessary and sufficient for the interaction <cite>Sato95, Li00, Ivanov03</cite>.

@@ Line 118: / Line 118: @@
 #Lee99 pmid=10660140
 #Li00 pmid=10918185
-#López-Ruano15 pmid=26344907
+#Lopez-Ruano15 pmid=26344907
 #Maekawa94 pmid=8287977
 #Maekawa99 pmid=9882613

@@ Line 78: / Line 78: @@
 * PTPN13 is a substrate of protein kinase A, but little is known about whether protein kinase A regulates PTPN13 <cite>Nedachi04</cite>.
-In addition, PTPN13 together with β-catenin regulates the quiescence of hematopoietic stem cells (HSCs) <cite>López-Ruano15</cite>.
+In addition, PTPN13 together with β-catenin regulates the quiescence of hematopoietic stem cells (HSCs) <cite>Lopez-Ruano15</cite>.
 ====== PTPN13 and cancer ======