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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Receptor-type tyrosine-protein phosphatase beta''' or '''VE-PTP''' is an [[enzyme]] specifically expressed in [[endothelial cell]]s  that in humans is encoded by the ''PTPRB'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRB protein tyrosine phosphatase, receptor type, B | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5787| accessdate = }}</ref><ref name = "Fachinger_1999" >{{cite journal | vauthors = Fachinger G, Deutsch U, Risau W | title = Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2 | journal = Oncogene | volume = 18 | issue = 43 | pages = 5948–5953 | date = Oct 1999 | pmid = 10557082 | doi = 10.1038/sj.onc.1202992 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PTPRB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ahs.
| PDB = {{PDB2|2ahs}}, {{PDB2|2h02}}, {{PDB2|2h03}}, {{PDB2|2h04}}, {{PDB2|2hc1}}, {{PDB2|2hc2}}, {{PDB2|2i3r}}, {{PDB2|2i3u}}, {{PDB2|2i4e}}, {{PDB2|2i4g}}, {{PDB2|2i4h}}, {{PDB2|2i5x}}
| Name = Protein tyrosine phosphatase, receptor type, B
| HGNCid = 9665
| Symbol = PTPRB
| AltSymbols =; DKFZp686E2262; DKFZp686H15164; FLJ44133; HPTP-BETA; HPTPB; MGC142023; MGC59935; PTPB; R-PTP-BETA
| OMIM = 176882
| ECnumber = 
| Homologene = 2125
| MGIid = 97809
| GeneAtlas_image1 = PBB_GE_PTPRB_205846_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0006796 |text = phosphate metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5787
    | Hs_Ensembl = ENSG00000127329
    | Hs_RefseqProtein = NP_002828
    | Hs_RefseqmRNA = NM_002837
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 69201231
    | Hs_GenLoc_end = 69317469
    | Hs_Uniprot = P23467
    | Mm_EntrezGene = 19263
    | Mm_Ensembl = ENSMUSG00000020154
    | Mm_RefseqmRNA = NM_029928
    | Mm_RefseqProtein = NP_084204
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 115679633
    | Mm_GenLoc_end = 115785122
    | Mm_Uniprot = 
  }}
}}
'''Protein tyrosine phosphatase, receptor type, B''', also known as '''PTPRB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRB protein tyrosine phosphatase, receptor type, B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5787| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
VE-PTP is a member of the classical [[protein tyrosine phosphatase]] (PTP) family. The deletion of the gene in mouse models was shown to be embryonically lethal,<ref>{{cite journal | vauthors = Bäumer S, Keller L, Holtmann A, Funke R, August B, Gamp A, Wolburg H, Wolburg-Buchholz K, Deutsch U, Vestweber D | title = Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development | journal = Blood | volume = 107 | issue = 12 | pages = 4754–62 | date = Jun 2006 | pmid = 16514057 | doi = 10.1182/blood-2006-01-0141 }}</ref> thus indicating that it is important for [[vasculogenesis]] and blood vessel development.  In addition, it was shown to participate in [[adherens junctions]] complex and regulate [[vascular permeability]].<ref>{{cite journal | vauthors = Broermann A, Winderlich M, Block H, Frye M, Rossaint J, Zarbock A, Cagna G, Linnepe R, Schulte D, Nottebaum AF, Vestweber D | title = Dissociation of VE-PTP from VE-cadherin is required for leukocyte extravasation and for VEGF-induced vascular permeability in vivo | journal = The Journal of Experimental Medicine | volume = 208 | issue = 12 | pages = 2393–401 | date = Nov 2011 | pmid = 22025303 | doi = 10.1084/jem.20110525 | pmc=3256962}}</ref><ref name="Soni"/> Recently, Soni et al. have shown that tyrosine phosphorylation of VE-PTP via [[Pyk2]] kinase downstream of [[STIM1]]-induced calcium entry mediates disassembly of the endothelial [[adherens junctions]].<ref name= "Soni">{{cite journal | vauthors = Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, Tiruppathi C | title = Pyk2 Phosphorylation of VE-PTP Downstream of STIM1 induced Ca2+ entry Regulates Disassembly of Adherens Junctions | journal = American Journal of Physiology. Lung Cellular and Molecular Physiology | volume =  | issue =  | page =  ajplung.00008.2017| date = Apr 2017 | pmid = 28385807 | doi = 10.1152/ajplung.00008.2017 }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular domain, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to receptor type PTP. The extracellular region of this PTP is composed of multiple fibronectin type_III repeats, which was shown to interact with neuronal receptor and cell adhesion molecules, such as contactin and tenascin C. This protein was also found to interact with sodium channels, and thus may regulate sodium channels by altering tyrosine phosphorylation status. The functions of the interaction partners of this protein implicate the roles of this PTP in cell adhesion, neurite growth, and neuronal differentiation.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRB protein tyrosine phosphatase, receptor type, B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5787| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
VE-PTP contains an extracellular domain composed of multiple fibronectin type_III repeats, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to R3 receptor subtype PTPs.
The extracellular region was shown to interact with the [[angiopoietin]] receptor [[Tie-2]]<ref name = "Fachinger_1999"/> and with the adhesion protein [[VE-cadherin]].<ref name="Soni"/><ref>{{cite journal | vauthors = Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G, Golding M, Shima DT, Deutsch U, Vestweber D | title = VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts | journal = The EMBO Journal | volume = 21 | issue = 18 | pages = 4885–4895 | date = Sep 2002 | pmid = 12234928 | doi = 10.1093/emboj/cdf497 | pmc=126293}}</ref>
 
VE-PTP was also found to interact with [[Grb2]] and [[plakoglobin]] through its cytoplasmatic domain.
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Ramachandran C, Aebersold R, Tonks NK, Pot DA | title = Sequential dephosphorylation of a multiply phosphorylated insulin receptor peptide by protein tyrosine phosphatases | journal = Biochemistry | volume = 31 | issue = 17 | pages = 4232–8 | year = 1992 | pmid = 1373652 | doi = 10.1021/bi00132a012 }}
| citations =
* {{cite journal | vauthors = Harder KW, Anderson LL, Duncan AM, Jirik FR | title = The gene for receptor-like protein tyrosine phosphatase (PTPRB) is assigned to chromosome 12q15→q21 | journal = Cytogenet. Cell Genet. | volume = 61 | issue = 4 | pages = 269–70 | year = 1993 | pmid = 1486802 | doi = 10.1159/000133419 }}
*{{cite journal  | author=Peles E, Schlessinger J, Grumet M |title=Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling. |journal=Trends Biochem. Sci. |volume=23 |issue= 4 |pages= 121-4 |year= 1998 |pmid= 9584610 |doi=  }}
* {{cite journal | vauthors = Krueger NX, Streuli M, Saito H | title = Structural diversity and evolution of human receptor-like protein tyrosine phosphatases | journal = EMBO J. | volume = 9 | issue = 10 | pages = 3241–52 | year = 1990 | pmid = 2170109 | pmc = 552056 | doi =  }}
*{{cite journal  | author=Dewang PM, Hsu NM, Peng SZ, Li WR |title=Protein tyrosine phosphatases and their inhibitors. |journal=Curr. Med. Chem. |volume=12 |issue= 1 |pages= 1-22 |year= 2005 |pmid= 15638728 |doi=  }}
* {{cite journal | vauthors = Gaits F, Li RY, Ragab A, Ragab-Thomas JM, Chap H | title = Increase in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cells | journal = Biochem. J. | volume = 311 | issue = Pt 1 | pages = 97–103 | year = 1995 | pmid = 7575486 | pmc = 1136124 | doi =  10.1042/bj3110097}}
*{{cite journal | author=Ramachandran C, Aebersold R, Tonks NK, Pot DA |title=Sequential dephosphorylation of a multiply phosphorylated insulin receptor peptide by protein tyrosine phosphatases. |journal=Biochemistry |volume=31 |issue= 17 |pages= 4232-8 |year= 1992 |pmid= 1373652 |doi= }}
* {{cite journal | vauthors = Feito MJ, Bragardo M, Buonfiglio D, Bonissoni S, Bottarel F, Malavasi F, Dianzani U | title = gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules | journal = Int. Immunol. | volume = 9 | issue = 8 | pages = 1141–7 | year = 1997 | pmid = 9263011 | doi = 10.1093/intimm/9.8.1141 }}
*{{cite journal | author=Harder KW, Anderson LL, Duncan AM, Jirik FR |title=The gene for receptor-like protein tyrosine phosphatase (PTPRB) is assigned to chromosome 12q15-->q21. |journal=Cytogenet. Cell Genet. |volume=61 |issue= 4 |pages= 269-70 |year= 1993 |pmid= 1486802 |doi= }}
* {{cite journal | vauthors = Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G, Golding M, Shima DT, Deutsch U, Vestweber D | title = VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts | journal = EMBO J. | volume = 21 | issue = 18 | pages = 4885–95 | year = 2002 | pmid = 12234928 | pmc = 126293 | doi = 10.1093/emboj/cdf497 }}
*{{cite journal  | author=De Vries L, Li RY, Ragab A, ''et al.'' |title=Expression of a truncated protein-tyrosine phosphatase mRNA in human lung. |journal=FEBS Lett. |volume=282 |issue= 2 |pages= 285-8 |year= 1991 |pmid= 1645282 |doi=  }}
*{{cite journal | author=Kaplan R, Morse B, Huebner K, ''et al.'' |title=Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 18 |pages= 7000-4 |year= 1990 |pmid= 2169617 |doi=  }}
*{{cite journal  | author=Krueger NX, Streuli M, Saito H |title=Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3241-52 |year= 1990 |pmid= 2170109 |doi=  }}
*{{cite journal | author=Gaits F, Li RY, Ragab A, ''et al.'' |title=Increase in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cells. |journal=Biochem. J. |volume=311 ( Pt 1) |issue= |pages= 97-103 |year= 1995 |pmid= 7575486 |doi=  }}
*{{cite journal  | author=Peles E, Nativ M, Campbell PL, ''et al.'' |title=The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin. |journal=Cell |volume=82 |issue= 2 |pages= 251-60 |year= 1995 |pmid= 7628014 |doi=  }}
*{{cite journal  | author=Sakurai T, Lustig M, Nativ M, ''et al.'' |title=Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta. |journal=J. Cell Biol. |volume=136 |issue= 4 |pages= 907-18 |year= 1997 |pmid= 9049255 |doi=  }}
*{{cite journal  | author=Peles E, Nativ M, Lustig M, ''et al.'' |title=Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions. |journal=EMBO J. |volume=16 |issue= 5 |pages= 978-88 |year= 1997 |pmid= 9118959 |doi= 10.1093/emboj/16.5.978 }}
*{{cite journal | author=Feito MJ, Bragardo M, Buonfiglio D, ''et al.'' |title=gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules. |journal=Int. Immunol. |volume=9 |issue= 8 |pages= 1141-7 |year= 1997 |pmid= 9263011 |doi=  }}
*{{cite journal  | author=Fachinger G, Deutsch U, Risau W |title=Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2. |journal=Oncogene |volume=18 |issue= 43 |pages= 5948-53 |year= 1999 |pmid= 10557082 |doi= 10.1038/sj.onc.1202992 }}
*{{cite journal  | author=Meng K, Rodriguez-Peña A, Dimitrov T, ''et al.'' |title=Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2603-8 |year= 2000 |pmid= 10706604 |doi= 10.1073/pnas.020487997 }}
*{{cite journal | author=Ratcliffe CF, Qu Y, McCormick KA, ''et al.'' |title=A sodium channel signaling complex: modulation by associated receptor protein tyrosine phosphatase beta. |journal=Nat. Neurosci. |volume=3 |issue= 5 |pages= 437-44 |year= 2000 |pmid= 10769382 |doi= 10.1038/74805 }}
*{{cite journal  | author=Adamsky K, Schilling J, Garwood J, ''et al.'' |title=Glial tumor cell adhesion is mediated by binding of the FNIII domain of receptor protein tyrosine phosphatase beta (RPTPbeta) to tenascin C. |journal=Oncogene |volume=20 |issue= 5 |pages= 609-18 |year= 2001 |pmid= 11313993 |doi= 10.1038/sj.onc.1204119 }}
*{{cite journal  | author=Cheburkin IuV, Kniazeva TG, Peter S, ''et al.'' |title=[Molecular portrait of human kidney carcinomas: the gene expression profiling of protein-tyrosine kinases and tyrosine phosphatases which controlled regulatory signals in the cells] |journal=Mol. Biol. (Mosk.) |volume=36 |issue= 3 |pages= 480-90 |year= 2002 |pmid= 12068634 |doi=  }}
*{{cite journal  | author=Nawroth R, Poell G, Ranft A, ''et al.'' |title=VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts. |journal=EMBO J. |volume=21 |issue= 18 |pages= 4885-95 |year= 2002 |pmid= 12234928 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5787}}
{{WikiDoc Sources}}
 
{{Protein tyrosine phosphatases}}
 
 
{{gene-12-stub}}

Latest revision as of 04:26, 25 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Receptor-type tyrosine-protein phosphatase beta or VE-PTP is an enzyme specifically expressed in endothelial cells that in humans is encoded by the PTPRB gene.[1][2]

Function

VE-PTP is a member of the classical protein tyrosine phosphatase (PTP) family. The deletion of the gene in mouse models was shown to be embryonically lethal,[3] thus indicating that it is important for vasculogenesis and blood vessel development. In addition, it was shown to participate in adherens junctions complex and regulate vascular permeability.[4][5] Recently, Soni et al. have shown that tyrosine phosphorylation of VE-PTP via Pyk2 kinase downstream of STIM1-induced calcium entry mediates disassembly of the endothelial adherens junctions.[5]

Interactions

VE-PTP contains an extracellular domain composed of multiple fibronectin type_III repeats, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to R3 receptor subtype PTPs. The extracellular region was shown to interact with the angiopoietin receptor Tie-2[2] and with the adhesion protein VE-cadherin.[5][6]

VE-PTP was also found to interact with Grb2 and plakoglobin through its cytoplasmatic domain.

References

  1. ↑ "Entrez Gene: PTPRB protein tyrosine phosphatase, receptor type, B".
  2. ↑ 2.0 2.1 Fachinger G, Deutsch U, Risau W (Oct 1999). "Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2". Oncogene. 18 (43): 5948–5953. doi:10.1038/sj.onc.1202992. PMID 10557082.
  3. ↑ Bäumer S, Keller L, Holtmann A, Funke R, August B, Gamp A, Wolburg H, Wolburg-Buchholz K, Deutsch U, Vestweber D (Jun 2006). "Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development". Blood. 107 (12): 4754–62. doi:10.1182/blood-2006-01-0141. PMID 16514057.
  4. ↑ Broermann A, Winderlich M, Block H, Frye M, Rossaint J, Zarbock A, Cagna G, Linnepe R, Schulte D, Nottebaum AF, Vestweber D (Nov 2011). "Dissociation of VE-PTP from VE-cadherin is required for leukocyte extravasation and for VEGF-induced vascular permeability in vivo". The Journal of Experimental Medicine. 208 (12): 2393–401. doi:10.1084/jem.20110525. PMC 3256962. PMID 22025303.
  5. ↑ 5.0 5.1 5.2 Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, Tiruppathi C (Apr 2017). "Pyk2 Phosphorylation of VE-PTP Downstream of STIM1 induced Ca2+ entry Regulates Disassembly of Adherens Junctions". American Journal of Physiology. Lung Cellular and Molecular Physiology: ajplung.00008.2017. doi:10.1152/ajplung.00008.2017. PMID 28385807.
  6. ↑ Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G, Golding M, Shima DT, Deutsch U, Vestweber D (Sep 2002). "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts". The EMBO Journal. 21 (18): 4885–4895. doi:10.1093/emboj/cdf497. PMC 126293. PMID 12234928.

Further reading


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