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Protein tyrosine phosphatase, receptor type, K

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 possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP was shown to mediate homophilic intercellular interaction, possibly through the interaction with beta- and gamma-catenin at adherens junctions. Expression of this gene was found to be stimulated by TGF-beta 1, which may be important for the inhibition of keratinocyte proliferation. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: EGFR, RPTPs, Pts, HAD, RPTPmu
Papers on PTPRK
Targeting RSPO3 Reduces Stem Cell Function in PTPRK-RSPO3 Colon Tumors.
In Cancer Discov, Feb 2016
UNASSIGNED: Inhibition of RSPO3 induces differentiation of PTPRK-RSPO3 fusion-positive colon tumors.
Targeting PTPRK-RSPO3 colon tumours promotes differentiation and loss of stem-cell function.
de Sauvage et al., San Francisco, United States. In Nature, Feb 2016
Here we show that targeting RSPO3 in PTPRK-RSPO3-fusion-positive human tumour xenografts inhibits tumour growth and promotes differentiation.
TGFβ responsive tyrosine phosphatase promotes rheumatoid synovial fibroblast invasiveness.
Bottini et al., Los Angeles, United States. In Ann Rheum Dis, Jan 2016
We describe that the transmembrane receptor PTPκ (RPTPκ), encoded by the transforming growth factor (TGF) β-target gene, PTPRK, promotes RA FLS invasiveness.
Whole-exome sequencing of breast cancer, malignant peripheral nerve sheath tumor and neurofibroma from a patient with neurofibromatosis type 1.
Yap et al., Singapore, Singapore. In Cancer Med, Dec 2015
which harbors two potential tumor suppressor genes, PTPRK and LAMA2, was also identified; this may increase tumor predisposition further.
Aberrant RSPO3-LGR4 signaling in Keap1-deficient lung adenocarcinomas promotes tumor aggressiveness.
Liu et al., Houston, United States. In Oncogene, Oct 2015
Recurrent, gain-of-expression gene fusions of RSPO2 (to EIF3E) and RSPO3 (to PTPRK) occur in a subset of human colorectal cancer.
Tumor vessel up-regulation of INSR revealed by single-cell expression analysis of the tyrosine kinome and phosphatome in human cancers.
Sjöblom et al., Uppsala, Sweden. In Am J Pathol, Jun 2015
Further, pan-cancer expression of AATK, PTPRK, and PTPRU and expression of PTPRS in a subset of tumors were observed.
Receptor-type protein tyrosine phosphatase κ directly dephosphorylates CD133 and regulates downstream AKT activation.
Kamijo et al., Chiba, Japan. In Oncogene, May 2015
Using yeast two-hybrid screening, we finally identified receptor-type protein tyrosine phosphatase κ (PTPRK) as a binding partner of CD133.
Evaluation of European coeliac disease risk variants in a north Indian population.
Trynka et al., New Delhi, India. In Eur J Hum Genet, Apr 2015
Using a transferability test, we further confirmed association at PFKFB3/PRKCQ (rs2387397, P=2.8 × 10(-4)) and PTPRK/THEMIS (rs55743914, P=3.4 × 10(-4)).
Notch and TGF-β pathways cooperatively regulate receptor protein tyrosine phosphatase-κ (PTPRK) gene expression in human primary keratinocytes.
Fisher et al., Ann Arbor, United States. In Mol Biol Cell, Apr 2015
Receptor protein tyrosine phosphatase-κ (PTPRK) specifically and directly dephosphorylates epidermal growth factor receptor (EGFR), thereby limiting EGFR function in primary human keratinocytes.
Receptor-type tyrosine-protein phosphatase κ directly targets STAT3 activation for tumor suppression in nasal NK/T-cell lymphoma.
Srivastava et al., Hong Kong, Hong Kong. In Blood, Apr 2015
In this study, we investigated whether receptor-type tyrosine-protein phosphatase κ (PTPRK), the only protein tyrosine phosphatase at 6q that contains a STAT3-specifying motif, negatively regulates STAT3 activation in NKTCL.
Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis.
Brady-Kalnay et al., Cleveland, United States. In Semin Cell Dev Biol, 2015
The R2B subfamily is composed of four members: PTPmu (PTPRM), PTPrho (PTPRT), PTPkappa (PTPRK), and PCP-2 (PTPRU).
RSPO fusion transcripts in colorectal cancer in Japanese population.
Sugimura et al., Hamamatsu, Japan. In Mol Biol Rep, 2014
In this study, we examined 75 primary CRCs and 121 primary lung cancers in the Japanese population for EIF3E-RSPO2 and PTPRK-RSPO3 fusion transcripts using RT-PCR and subsequent sequencing analyses.
A whole genomic scan to detect selection signatures between Berkshire and Korean native pig breeds.
Kim et al., Ch'ŏngju, South Korea. In J Anim Sci Technol, 2013
Results revealed that 19 candidate genes were enriched in phosphate metabolism (GO: 0006796; ADCK1, ACYP1, CAMK2D, CDK13, CDK13, ERN1, GALK2, INPP1; MAK, MAP2K5, MAP3K1, MAPK14, P14KB, PIK3C3, PRKC1, PTPRK, RNASEL, THBS1, BRAF, VRK1).
The lysyl oxidase propeptide interacts with the receptor-type protein tyrosine phosphatase kappa and inhibits β-catenin transcriptional activity in lung cancer cells.
Sonenshein et al., Boston, United States. In Mol Cell Biol, 2011
RPTP-kappa is proteolytically processed to isoforms that have opposing effects on beta-catenin activity.
Galectin-3 binding protein promotes cell motility in colon cancer by stimulating the shedding of protein tyrosine phosphatase kappa by proprotein convertase 5.
Ko et al., Taejŏn, South Korea. In Biochem Biophys Res Commun, 2011
PTPkappa was scissored by the processed form of proprotein convertase 5, and galectin-3 binding protein which is over-produced in colon cancer cells and tissues.
Contiguous gene deletion of Ptprk and Themis causes T-helper immunodeficiency (thid) in the LEC rat.
Agui et al., Sapporo, Japan. In Biomed Res, 2010
Contiguous gene deletion of Ptprk and Themis causes T-helper immunodeficiency (thid) in the LEC rat.
Receptor type protein tyrosine phosphatase-kappa mediates cross-talk between transforming growth factor-beta and epidermal growth factor receptor signaling pathways in human keratinocytes.
Fisher et al., Ann Arbor, United States. In Mol Biol Cell, 2010
These data describe a novel mechanism of cross-talk between EGFR and TGF-beta pathways, in which RPTP-kappa functions to integrate growth-promoting and growth-inhibiting signaling pathways.
The effect of receptor protein tyrosine phosphatase kappa on the change of cell adhesion and proliferation induced by N-acetylglucosaminyltransferase V.
Zha et al., Shanghai, China. In J Cell Biochem, 2010
Our results suggest that GnT-V could decrease human hepatoma SMMC-7721 cell adhesion and promote cell proliferation partially through RPTPkappa.
A transposon-based genetic screen in mice identifies genes altered in colorectal cancer.
Largaespada et al., Minneapolis, United States. In Science, 2009
The screen also identified 17 candidate genes that had not previously been implicated in CRC, including POLI, PTPRK, and RSPO2.
Del(6)(q22) and BCL6 rearrangements in primary CNS lymphoma are indicators of an aggressive clinical course.
Remstein et al., Olympia, United States. In J Clin Oncol, 2008
Several genetic changes including BCL6 rearrangements and deletion of 6q22, containing the putative tumor suppressor gene PTPRK, are potential risk predictors.
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