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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Protein tyrosine phosphatase, receptor type, T

PTPRT, RPTPrho, receptor protein tyrosine phosphatase SHP-2
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 intracellular catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP (MAM) domain, Ig-like and fibronectin type III-like repeats. The protein domain structure and the expression pattern of the mouse counterpart of this PTP suggest its roles in both signal transduction and cellular adhesion in the central nervous system. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: NS1, Rhodopsin, RPTPs, Pts, CAN
Papers on PTPRT
Genetic alterations of protein tyrosine phosphatases in human cancers.
Wang et al., Shanghai, China. In Oncogene, Aug 2015
Among these mutated PTPs, PTP receptor T (PTPRT) appears to be the most frequently mutated PTP in human cancers.
Frequent promoter hypermethylation of PTPRT increases STAT3 activation and sensitivity to STAT3 inhibition in head and neck cancer.
Grandis et al., Pittsburgh, United States. In Oncogene, Jun 2015
Instead, STAT3 may be activated by loss-of-function of negative regulators of STAT3, including by promoter hypermethylation of PTPRT.
Protein tyrosine phosphatase PTPRT as a regulator of synaptic formation and neuronal development.
Lee, Taejŏn, South Korea. In Bmb Rep, May 2015
PTPRT/RPTPρ is the most recently isolated member of the type IIB receptor-type protein tyrosine phosphatase family and its expression is restricted to the nervous system.
Identification of MicroRNAs and target genes involvement in hepatocellular carcinoma with microarray data.
Cai et al., In Hepatogastroenterology, Mar 2015
The differentially expressed hsa-miR-106b was chosen for further analysis and PTPRT (Receptor-type tyrosine-protein phosphatase T) was its potential target gene.
Autoimmune liver disease in Noonan Syndrome.
Briuglia et al., Messina, Italy. In Eur J Med Genet, Mar 2015
In approximately 50% of cases, the disease is caused by missense mutations in the PTPN11 gene on chromosome 12, resulting in a gain of function of the non-receptor protein tyrosine phosphatase SHP-2 protein.
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).
Association analysis identifies new risk loci for congenital heart disease in Chinese populations.
Hu et al., Nanjing, China. In Nat Commun, 2014
(rs2433752, upstream of TBX3 and TBX5, Pall=1.04 × 10(-10)) and 20q12 (rs490514, in PTPRT, Pall=1.20 × 10(-13)).
Copy number alterations of chromosomal regions enclosing protein tyrosine phosphatase receptor-like genes in colorectal cancer.
Sasiadek et al., Wrocław, Poland. In Pathol Res Pract, 2014
In a previous study, we have described protein tyrosine phosphatase receptor type T, M, Z1 and Q genes (PTPRT, PTPRM, PTPRZ1 and PTPRQ) hypermethylated in sporadic colorectal cancer.
The Functional Variant in the 3'UTR of PTPRT with the Risk of Esophageal Squamous Cell Carcinoma in a Chinese Population.
Huang et al., Kunshan, China. In Cell Physiol Biochem, 2014
BACKGROUND/AIMS: PTPRT is an essential tumor suppressor that plays crucial roles in regulating the mechanisms of tumorigenesis.
Large-scale characterization of DNA methylation changes in human gastric carcinomas with and without metastasis.
Deng et al., Beijing, China. In Clin Cancer Res, 2014
These genes included BMP3, BNIP3, CDKN2A, ECEL1, ELK1, GFRA1, HOXD10, KCNH1, PSMD10, PTPRT, SIGIRR, SRF, TBX5, TFPI2, and ZNF382.
PTPRT regulates high-fat diet-induced obesity and insulin resistance.
Wang et al., Cleveland, United States. In Plos One, 2013
Here, we report that protein tyrosine phosphatase receptor T (PTPRT) knockout mice are resistant to high-fat diet-induced obesity.
Clonal architectures and driver mutations in metastatic melanomas.
Weber et al., Saint Louis, United States. In Plos One, 2013
Extension studies using tumors from another 96 patients discovered a large number of truncation mutations in tumor suppressors (TP53 and RB1), protein phosphatases (e.g., PTEN, PTPRB, PTPRD, and PTPRT), as well as chromatin remodeling genes (e.g., ASXL3, MLL2, and ARID2).
Structural stability of human protein tyrosine phosphatase ρ catalytic domain: effect of point mutations.
Chiaraluce et al., Roma, Italy. In Plos One, 2011
The catalytic domain point mutants show a decreased thermal and thermodynamic stability and decreased activation energy relative to phosphatase activity, when compared to wild- type
Tumour suppressor function of protein tyrosine phosphatase receptor-T.
Wang et al., Cleveland, United States. In Biosci Rep, 2011
[review] High-throughput mutational analysis identifies loss-of-function mutations in six PTPs in human colon cancers, providing critical cancer genetics evidence that PTPs can act as tumour suppressor genes.
Tyrosine phosphatases as a superfamily of tumor suppressors in colorectal cancer.
Sasiadek et al., Wrocław, Poland. In Acta Biochim Pol, 2010
Mutational analysis of the tyrosine phosphatome in CRCs has identified somatic mutations in PTPRG, PTPRT, PTPN3, PTPN13 and PTPN14.
Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T.
Wang et al., Chengdu, China. In Proc Natl Acad Sci U S A, 2010
Data show that paxillin is a direct substrate of PTPRT and that PTPRT specifically regulates paxillin phosphorylation at tyrosine residue 88(Y88).
Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.
Lee et al., Taejŏn, South Korea. In Embo J, 2009
brain-specific PTPRT regulates synapse formation through interaction with cell adhesion molecules, and this function and the phosphatase activity are attenuated through tyrosine phosphorylation by the synaptic tyrosine kinase Fyn.
Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T.
Wang et al., Cleveland, United States. In Proc Natl Acad Sci U S A, 2007
STAT3 is a substrate of receptor protein tyrosine phosphatase T
Mutational analysis of the tyrosine phosphatome in colorectal cancers.
Velculescu et al., Baltimore, United States. In Science, 2004
A mutational analysis of the tyrosine phosphatase gene superfamily in human cancers identified 83 somatic mutations in six PTPs (PTPRF, PTPRG, PTPRT, PTPN3, PTPN13, PTPN14), affecting 26% of colorectal cancers and a smaller fraction of lung, breast, and gastric cancers.
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