PTPRS

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 region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains (D1 and D2), and thus represents a receptor-type PTP. D1 is catalytically active, while D2 is catalytically inactive. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Rem2 signaling affects neuronal structure and function in part by regulation of gene expression. Molecular and Cellular NeuroscienceStudies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.

A PTPRS protein mimetic may improve muscular and bladder control in rats with spinal cord injuries.{{cite web |url=https://www.nbcnews.com/health/health-news/unprecedented-drug-may-help-heal-damaged-spine-n261116|title='Unprecedented': Drug May Help Heal Damaged Spine|newspaper=NBC|date=3 December 2014|author=Maggie Fox|access-date=December 8, 2014}}

PTPRS has been shown to interact with:

• chondroitin sulphate proteoglycans,{{cite journal | vauthors = Lang BT, Cregg JM, DePaul MA, Tran AP, Xu K, Dyck SM, Madalena KM, Brown BP, Weng Y, Li S, Karimi-Abdolrezaee S, Busch SA, Shen Y, Silver J | title = Modulation of the proteoglycan receptor PTPσ promotes recovery after spinal cord injury | journal = Nature | volume = 518| issue = 7539| pages = 404–8| year = 2014 | pmid = 25470046 | doi = 10.1038/nature13974 | pmc=4336236}}
• PTPRD,{{cite journal | vauthors = Wallace MJ, Fladd C, Batt J, Rotin D | title = The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma | journal = Mol. Cell. Biol. | volume = 18 | issue = 5 | pages = 2608–16 | date = May 1998 | pmid = 9566880 | pmc = 110640 | doi = 10.1128/MCB.18.5.2608}} glial-derived and
• liprin-alpha-1.{{cite journal | vauthors = Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M | title = Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins | journal = J. Biol. Chem. | volume = 273 | issue = 25 | pages = 15611–20 | date = Jun 1998 | pmid = 9624153 | doi = 10.1074/jbc.273.25.15611| doi-access = free }}
• NME2.{{cite journal | vauthors = Hamasaki H, Fujitani M, Yamashita T | title = NME2 associates with PTPσ to transduce signals from chondroitin sulfate proteoglycans | journal = Biochemical and Biophysical Research Communications | volume = 471 | issue = 4 | pages = 522–7 | date = March 2016 | pmid = 26896769 | doi = 10.1016/j.bbrc.2016.02.042 }}

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• {{cite journal | vauthors = Wallace MJ, Fladd C, Batt J, Rotin D | title = The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma. | journal = Mol. Cell. Biol. | volume = 18 | issue = 5 | pages = 2608–16 | year = 1998 | pmid = 9566880 | pmc = 110640 | doi = 10.1128/MCB.18.5.2608}}
• {{cite journal | vauthors = Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M | title = Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. | journal = J. Biol. Chem. | volume = 273 | issue = 25 | pages = 15611–20 | year = 1998 | pmid = 9624153 | doi = 10.1074/jbc.273.25.15611 | doi-access = free }}
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{{Protein tyrosine phosphatases}}

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