Phosphatase Subfamily PTPRB - Revision history

Gerard at 23:52, 4 April 2017

2017-04-04T23:52:10Z

Gerard: /* Evolution */

2017-04-04T23:50:13Z

‎Evolution

Gerard: /* Evolution */

2017-04-03T00:51:13Z

‎Evolution

Gerard: /* Domain Structure */

2017-04-03T00:49:52Z

‎Domain Structure

Gerard: /* Domain Structure */

2017-04-03T00:48:44Z

‎Domain Structure

Gerard: /* Domain Structure */

2017-04-03T00:45:21Z

‎Domain Structure

Gerard: /* Domain Structure */

2017-04-03T00:43:31Z

‎Domain Structure

Mark: /* References */

2017-01-06T14:13:58Z

‎References

Mark: /* PTPRJ (CD148/DEP1/RPTP eta) */

2017-01-06T14:13:06Z

‎PTPRJ (CD148/DEP1/RPTP eta)

Gerard: /* PTPRQ */

2016-12-22T01:43:03Z

‎PTPRQ

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 ===Evolution===
-PTPRB is found across metazoa, often with multiple members per species. Human members are PTPRB, PTPRH, PTPRJ, PTPRO, and PTPRQ, while C. elegans has a single gene, dep-1 and Drosophila has two: Ptp4E and Ptp10D. Distinct PTPRB and PTPRQ orthologs are seen in invertebrate chordates.
+PTPRB is found across metazoa, often with multiple members per species. Human members are PTPRB, PTPRH, PTPRJ, PTPRO, and PTPRQ, while C. elegans has a single gene, dep-1 and Drosophila has two: Ptp4E and Ptp10D. Distinct PTPRB and PTPRQ orthologs are seen in invertebrate chordates <cite>Chicote</cite>.
 ===Domain Structure===
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 #Chabot09 pmid=18936167
 #Chen06 pmid=16888096
 #Fachinger99 pmid=10557082
 #Fiorillo04 pmid=20538612

@@ Line 5: / Line 5: @@
 ===Evolution===
-PTPRB is found across metazoa, often with multiple members per species. Human members are PTPRB, PTPRH, PTPRJ, PTPRO, and PTPRQ, while C. elegans has a single gene, dep-1 and Drosophila has two: Ptp4E and Ptp10D.
+PTPRB is found across metazoa, often with multiple members per species. Human members are PTPRB, PTPRH, PTPRJ, PTPRO, and PTPRQ, while C. elegans has a single gene, dep-1 and Drosophila has two: Ptp4E and Ptp10D. Distinct PTPRB and PTPRQ orthologs are seen in invertebrate chordates.
 ===Domain Structure===

@@ Line 5: / Line 5: @@
 ===Evolution===
-PTPRB is found across metazoa, often with multiple members per species. Human members are PTPRB, PTPRH, PTPRJ, PTPRO, and PTPRQ, while C. elegans has a single gene, dep-1 and Drosophila has two: PTP4E and PTP10D.
+PTPRB is found across metazoa, often with multiple members per species. Human members are PTPRB, PTPRH, PTPRJ, PTPRO, and PTPRQ, while C. elegans has a single gene, dep-1 and Drosophila has two: Ptp4E and Ptp10D.
 ===Domain Structure===

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 * Human PTPRQ has a shorter isoform with a signal peptide (NP_001138498.1) and a longer form with an additional two FN3 domains, but no signal peptide (XP_016874763.1). These have been seen to be differentially localized in cells <cite>Seifert03</cite>.
 * Human PTPRB has a shorter, signal peptide-containing isoform (XP_011525485.1) and a longer isoform whose N-terminal extension encodes a lectin domain (XP_016882549.1).
 ===Functions===

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 ===Domain Structure===
-The canonical domain structure is multiple fibronectin type III (Fn3) domains in the extracellular region and a single cytoplasmic phosphatase domain.
+The canonical domain structure is multiple fibronectin type III (Fn3) domains in the extracellular region and a single cytoplasmic phosphatase domain. Several members have differential promoter usage and alternative splicing to create isoforms that contain or lack a signal peptide:
-Human PTPRH has two isoforms, each with a unique promoter and first exon. XP_011525485.1 encodes an isoform with a signal peptide, and XP_016882549.1 is a slightly longer N-terminus that lacks a signal peptide.
+* Human PTPRH has two isoforms, each with a unique promoter and first exon. XP_011525485.1 encodes an isoform with a signal peptide, and XP_016882549.1 is a slightly longer N-terminus that lacks a signal peptide.
-PTPRQ also has a shorter isoform with a signal peptide (NP_001138498.1) and a longer form with an additional two FN3 domains, but no signal peptide (XP_016874763.1). These have been seen to be differentially localized in cells <cite>Seifert03</cite>
+* Human PTPRQ has a shorter isoform with a signal peptide (NP_001138498.1) and a longer form with an additional two FN3 domains, but no signal peptide (XP_016874763.1). These have been seen to be differentially localized in cells <cite>Seifert03</cite>.
 ===Functions===

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 #Behjati14 pmid=24633157
 #Berset05 pmid=15901674
 #Bohmer13 pmid=23650535
 #Brunner11 pmid=21304107

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 PTPRJ has ligands:
 * [http://en.wikipedia.org/wiki/Thrombospondin_1 Thrombospondin-1] <cite>Takahashi12</cite>, an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. It is a natural inhibitor of neovascularization and tumorigenesis in healthy tissue.
 * [http://en.wikipedia.org/wiki/SDC2 Syndecan-2] <cite>Whiteford11</cite>, a heparan sulfate proteoglycan participates in cell proliferation, cell migration and cell-matrix interactions via its receptor for extracellular matrix proteins.
 PTPRJ dephosphorylates  growth factor receptors as well as other substrates:
 * [http://en.wikipedia.org/wiki/Epidermal_growth_factor_receptor EGFR], a subfamily of receptor tyrosine kinases (RTKs). PTPRJ dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex. Interestingly, the interactions of DEP-1 and EGFR are followed by physical segregation: whereas EGFR undergoes endocytosis, DEP-1 remains confined to the cell surface <cite>Tarcic09</cite>.
 * [http://en.wikipedia.org/wiki/VEGF_receptors VEGFR2], a member of VEGFR subfamily (not EGFR subfamily), receptor tyrosine kinase family <cite>Chabot09</cite>.
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 * [http://en.wikipedia.org/wiki/CTNND1 CTNND1/p120 catenin], a member of the Armadillo protein family, which function in adhesion between cells and signal transduction <cite>Holsinger02</cite>.
 * PTPRJ can reduce phospholipase Cgamma1 ([http://en.wikipedia.org/wiki/PLCG1 PLCG1]) and LAT phosphorylation and inhibit T-cell receptor signal transduction <cite>Baker01</cite>.. But, it is unclear whether they are PTPRJ's physiological substrates. In fact, PTPRC/CD45 also reduces PLCG1 phosphorylation.
 ====== PTPRO (GLEPP1/PTP phi) ======

← Older revision		Revision as of 01:43, 22 December 2016
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	PTPRQ has also been shown to involved in differentiation during adipogenesis of human mesenchymal stem cells <cite>Jung09</cite> and regulation the adhesion and migration of mesangial cells in response to injury <cite>Wright98</cite>.		PTPRQ has also been shown to involved in differentiation during adipogenesis of human mesenchymal stem cells <cite>Jung09</cite> and regulation the adhesion and migration of mesangial cells in response to injury <cite>Wright98</cite>.
		+
		+	PTPRQ is seen in all vertebrates, and a likely ortholog (XP_002123247.3) also exists in Ciona intestinalis.

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