Phosphatase Subfamily PTPRD - Revision history

Gerard at 21:42, 21 December 2016

2016-12-21T21:42:50Z

Gerard at 20:28, 21 December 2016

2016-12-21T20:28:01Z

Gerard: /* Evolution */

2016-12-21T20:25:58Z

‎Evolution

Mark: /* References */

2015-05-24T05:15:44Z

‎References

Mark: /* PTPRS (RPTPsigma/RPTPσ) */

2015-05-24T05:15:17Z

‎PTPRS (RPTPsigma/RPTPσ)

Mark: /* PTPRS (RPTPsigma/RPTPσ) */

2015-05-24T05:12:57Z

‎PTPRS (RPTPsigma/RPTPσ)

Mark: /* PTPRS (RPTPsigma) */

2015-05-24T05:12:08Z

‎PTPRS (RPTPsigma)

Mark: /* References */

2015-04-25T20:35:32Z

‎References

Mark: /* PTPRD (RPTPdelta, PTPδ) */

2015-04-25T20:35:08Z

‎PTPRD (RPTPdelta, PTPδ)

Mark: /* PTPRD (RPTPdelta) */

2015-04-25T20:33:02Z

‎PTPRD (RPTPdelta)

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 __NOTOC__
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPRD|Subfamily PTPRD]]
 PTPRD phosphatases localize to axonal growth cones, regulating neuronal growth and guidance and participating in excitatory synapse formation and maintenance in vertebrates as well as invertebrates.
-PTPRD subfamily phosphatases localize to axonal growth cones, regulating neuronal growth and guidance and participating in excitatory synapse formation and maintenance in vertebrates as well as invertebrates.
 ===Evolution===

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 ===Evolution===
-PTPRD subfamily is found in holozoa (metazoa plus choanoflagellates). PTPRD has three members in human and most vertebrates: PTPRD, PTPRF and PTPRS. It has single member in most invertebrate metazoa but greatly expanded in sponge.
+PTPRD is found in holozoa (metazoa plus choanoflagellates). PTPRD has three members in human and most vertebrates: PTPRD, PTPRF and PTPRS. It has single member in most invertebrate metazoa but greatly expanded in sponge.
 ===Domain Structure===
-All three members of PTPRD subfamily in human has twin intracellular PTP phosphatase domains, and extracellular Ig domains and FN3 domains. Each of them have multiple alternative splicing isoforms <cite>Pulido95, OGrady94, Endo96</cite>.
+All three human PTPRDs have twin intracellular PTP phosphatase domains, and extracellular Ig domains and FN3 domains. Each of them have multiple alternative splicing isoforms <cite>Pulido95, OGrady94, Endo96</cite>. Invertebrate homologs have a similar architecture, though many gene models are incomplete.
 ===Functions===
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 The best characterized member of the three human genes in the subfamily is PTPRF, aka LAR. Knock-down of PTPRF by siRNA induced post-receptor insulin resistance with the insulin-induced activation of PKB/Akt and MAP kinases markedly inhibited. But, the phosphorylation and dephosphorylation of the IR and insulin receptor substrate (IRS) proteins were unaffected by PTPRF knock-down <cite>Mander05</cite>.
-PTPRF dephosphorylates phosphorylated tyrosine residues in both the COOH terminus and kinase domain of Fyn in vitro. It binds to Fyn Src homology 2 domain when its 2nd phosphatase was tyrosine phosphorylated by Fyn tyrosine kinase. In addition to Fyn kinase, PTPRF mutants, with Cys to Ser mutation in the catalytic center of 1st phosphatase domain, can bind to tyrosine-phosphorylated Lck kinase <cite>Tsujikawa02</cite>.
+PTPRF dephosphorylates tyrosine residues in both the C-terminus and kinase domain of Fyn in vitro. It binds to Fyn SH2 domain when its 2nd phosphatase was tyrosine phosphorylated by Fyn tyrosine kinase. In addition to Fyn kinase, PTPRF mutants, with Cys to Ser mutation in the catalytic center of 1st phosphatase domain, can bind to tyrosine-phosphorylated Lck kinase <cite>Tsujikawa02</cite>.
 PTPRF dephosphorylates Death-associated protein kinase (DAPK) at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK <cite>Wang07</cite>. (Note: Upon EGF stimulation, a rapid Src activation leads to subsequent LAR downregulation.)

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 ===Evolution===
-PTPRD subfamily is found in holozoan (metazoan plus it closest relative choanoflagellate). PTPRD subfamily has three gene members in human and most vertebrates: PTPRD, PTPRF and PTPRS. It has single member in most invertebrate metazoan and is under intensive studies in frtui fly. Interestingly, it greatly expanded in sponge.
+PTPRD subfamily is found in holozoa (metazoa plus choanoflagellates). PTPRD has three members in human and most vertebrates: PTPRD, PTPRF and PTPRS. It has single member in most invertebrate metazoa but greatly expanded in sponge.
 ===Domain Structure===

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 ===References===
 <biblio>
 #Pulido95 pmid=8524829
 #OGrady94 pmid=7929208

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 PTPRS reduce EGFR phosphorylation and therefore modulates signaling of the epidermal growth factor receptor in A431 cells <cite>Bohmer99</cite>. Frequent deletion of PTPRS was found in head and neck cancers. PTPRS loss promoted EGFR/PI3K pathway activation, modulated resistance to EGFR inhibition, and strongly determined survival in lung cancer patients with activating EGFR mutations <cite>Morris11</cite>.
-PTPRS-deficient mice exhibit neurological and neuroendocrine defects <cite>Elchebly99, Wallace99</cite>. PTPRS interacts with interact with proteoglycans heparan sulfate proteoglycans (HSPGs) and chondroitin sulfate proteoglycans (CSPGs) through extracellular region. The proteoglycans exert opposing effects on neuronal extension by competing to control the oligomerization of PTPRS <cite>Coles11</cite>.
+PTPRS-deficient mice exhibit neurological and neuroendocrine defects <cite>Elchebly99, Wallace99</cite>. PTPRS interacts with proteoglycans heparan sulfate proteoglycans (HSPGs) and chondroitin sulfate proteoglycans (CSPGs) through extracellular region. The proteoglycans exert opposing effects on neuronal extension by competing to control the oligomerization of PTPRS <cite>Coles11</cite>. The proteoglycan switch is a putative target of rheumatoid arthritis therapy <cite>Doody15</cite>.
 PTPRS is involved in the regulation of autophagy. Loss of PTPRS increases levels of cellular Phosphatidylinositol-3-phosphate (PtdIns3P) <cite>Martin11</cite>. However, it is unclear whether PtdIns3P is its physiological substrate.

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 PTPRD is also involved in synaptic differentiation. It can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to interleukin-1 receptor accessory protein (IL-1RAcP) and IL-1RAcP-like-1 (IL1RAPL1) in a splicing-dependent manner <cite>Yamagata15</cite>.
-===== PTPRS (RPTPsigma) =====
+===== PTPRS (RPTPsigma/RPTPσ) =====
 PTPRS reduce EGFR phosphorylation and therefore modulates signaling of the epidermal growth factor receptor in A431 cells <cite>Bohmer99</cite>. Frequent deletion of PTPRS was found in head and neck cancers. PTPRS loss promoted EGFR/PI3K pathway activation, modulated resistance to EGFR inhibition, and strongly determined survival in lung cancer patients with activating EGFR mutations <cite>Morris11</cite>.

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 #Elchebly99 pmid=10080191
 #Coles11 pmid=21454754
 </biblio>

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 ===== PTPRD (RPTPdelta, PTPδ) =====
 Human PTPRD is a tumor suppressor that is frequently inactivated and mutated in glioblastoma and other human cancers. PTPRD dephosphorylates STAT3 Y705, a residue that must be phosphorylated for STAT3 to be active <cite>veeriah09</cite>.  PTPRD loss can cause of aberrant STAT3 activation in gliomas <cite>ortiz14</cite>. Human PTPRD is also associated with [http://en.wikipedia.org/wiki/Restless_legs_syndrome restless legs syndrome] <cite>schormair08</cite>, but the underlying mechanism is unclear. PTPRD interacts with MIM-B, a putative metastasis suppressor protein binding to actin <cite>woodings03</cite>. It is not clear whether MIM-B is its substrate. The 2nd phosphatase domain of PTPRD can bind to inhibit the 1st phosphatase domain of PTPRS <cite>wallace98</cite>.
 ===== PTPRS (RPTPsigma) =====

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 PTPRF associates with [http://en.wikipedia.org/wiki/C-Met c-Met], and purified PTPRF dephosphorylates tyrosine-phosphorylated c-Met in in vitro <cite>Machide06</cite>. Other PTPs also have shown activities toward c-Met <cite>Sangwan08</cite>, and it is unclear whether c-Met is PTPRF's physiological substrate.
-===== PTPRD (RPTPdelta) =====
+===== PTPRD (RPTPdelta, PTPδ) =====
 Human PTPRD is a tumor suppressor that is frequently inactivated and mutated in glioblastoma and other human cancers. PTPRD dephosphorylates STAT3 Y705, a residue that must be phosphorylated for STAT3 to be active <cite>veeriah09</cite>.  PTPRD loss can cause of aberrant STAT3 activation in gliomas <cite>ortiz14</cite>. Human PTPRD is also associated with [http://en.wikipedia.org/wiki/Restless_legs_syndrome restless legs syndrome] <cite>schormair08</cite>, but the underlying mechanism is unclear. PTPRD interacts with MIM-B, a putative metastasis suppressor protein binding to actin <cite>woodings03</cite>. It is not clear whether MIM-B is its substrate. The 2nd phosphatase domain of PTPRD can bind to inhibit the 1st phosphatase domain of PTPRS <cite>wallace98</cite>.