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Protein tyrosine phosphatase, receptor type, M

RPTPmu, Ptprm
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 has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion. Alternative splicing results in multiple transcripts encoding distinct isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: RPTPs, alpha2-macroglobulin, Pts, fibronectin, PTPRK
Papers on RPTPmu
microRNA-103/107 Family Regulates Multiple Epithelial Stem Cell Characteristics.
Lavker et al., Chicago, United States. In Stem Cells, May 2015
This miRNA family also regulates keratinocyte cell-cell communication by targeting: (a) the scaffolding protein NEDD9, preserving E-cadherin-mediated cell adhesion; and (b) the tyrosine phosphatase PTPRM, which negatively regulates connexin 43-based gap junctions.
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).
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.
Genome Wide Methylome Alterations in Lung Cancer.
Spivack et al., New York City, United States. In Plos One, 2014
Of the canonical changes noted, promoter (PR) DM loci with reciprocal changes in expression in adenocarcinomas included HBEGF, AGER, PTPRM, DPT, CST1, MELK; DM GB loci with concordant changes in expression included FOXM1, FERMT1, SLC7A5, and FAP genes.
Identification of lung cancer oncogenes based on the mRNA expression and single nucleotide polymorphism profile data.
Chen et al., In Neoplasma, 2014
Besides, PIK3R1 (phosphoinositide-3-kinase, regulatory subunit 1), RORA (RAR-related orphan receptor A), MAGI3 (membrane associated guanylate kinase, WW and PDZ domain containing 3), PTPRM (protein tyrosine phosphatase, receptor type, M), and BMP6 (bone morphogenetic protein 6) were the hub genes in PPI network.
Loss of PTPRM associates with the pathogenic development of colorectal adenoma-carcinoma sequence.
Chen et al., Taipei, Taiwan. In Sci Rep, 2014
We performed quantitative PCR analysis of the genomic and complementary DNA derived from primary mucosa, adenoma, and carcinoma samples, and confirmed the recurrent loss and down-regulation of PTPRM in colon adenomas and carcinomas.
DNA methylation of membrane-bound tyrosine phosphatase genes in acute lymphoblastic leukaemia.
Garcia-Manero et al., Sydney, Australia. In Leukemia, 2014
PTPRG was methylated in 63% of ALL samples, PTPRK in 47%, PTPRM in 64% and PTPRO in 54% of cases, with most ALL samples containing methylation at multiple phosphatase loci.
Protein tyrosine phosphatase receptor-like genes are frequently hypermethylated in sporadic colorectal cancer.
Sasiadek et al., Wrocław, Poland. In J Hum Genet, 2013
In our study, we have investigated the methylation status of four PTPRs: PTPRM, PTPRT, PTPRR and PTPRZ1, which were pre-selected using microarray techniques as being alternatively methylated in sporadic colorectal cancer (CRC).
Extensive somatic L1 retrotransposition in colorectal tumors.
Kazazian et al., Baltimore, United States. In Genome Res, 2012
Numerous genes with a role in tumorigenesis were targeted, including ODZ3, ROBO2, PTPRM, PCM1, and CDH11.
A systematic evaluation of miRNA:mRNA interactions involved in the migration and invasion of breast cancer cells.
Shi et al., Nanchang, China. In J Transl Med, 2012
The integrated analysis of miRNA and mRNA expression identified 35 known and novel target genes of miR-200c, miR-205, and mir-375, including CFL2, LAMC1, TIMP2, ZEB1, CDH11, PRKCA, PTPRJ, PTPRM, LDHB, and SEC23A.
Replication study of 10 genes showing evidence for association with multiple sclerosis: validation of TMEM39A, IL12B and CBLB [correction of CLBL] genes.
Urcelay et al., Spain. In Mult Scler, 2012
RESULTS: Replication extended to the following polymorphisms: PKN2 (rs305217), GTF2B (rs7538427), EPHA4 (rs1517440), YTHDF3 (rs12115114), ANKFN1 (rs17758761) and PTPRM (rs4798571), which did not reach the threshold of significance in a follow-up of the first genome-wide association study (GWAS) conducted in multiple sclerosis; TMEM39A (rs1132200), which appeared as a newly identified susceptibility gene in the same study; a gene previously reaching GWAS significance in Italy, CBLB (rs9657904); IL12B (rs6887695, rs10045431), a susceptibility gene shared by diverse autoimmune diseases and, finally, another gene showing inconclusive association with multiple sclerosis, CNR1 (rs1049353).
Protein tyrosine phosphatase mu regulates glioblastoma cell growth and survival in vivo.
Brady-Kalnay et al., Cleveland, United States. In Neuro Oncol, 2012
Loss of PTPmu by proteolysis causes glioblastoma.
miR-221/222 overexpession in human glioblastoma increases invasiveness by targeting the protein phosphate PTPμ.
Condorelli et al., Napoli, Italy. In Oncogene, 2012
Results suggest that miR-221 and -222 regulate glioma tumorigenesis at least in part through the control of PTPmu protein expression.
Non-housekeeping genes expressed in human trabecular meshwork cell cultures.
Elahi et al., Dāmghān, Iran. In Mol Vis, 2011
Ten genes identified here, ALDH1A1 (aldehyde dehydrogenase 1 family, member A1), CDH11 (cadherin 11, type 2, OB-cadherin), CXCR7 (chemokine (C-X-C motif) receptor 7), CHI3L1 (chitinase 3-like 1), FGF2 (fibroblast growth factor 2), GNG11 (guanine nucleotide binding protein [G protein], gamma 11), IGFBP5 (insulin-like growth factor binding protein 5), PTPRM (protein tyrosine phosphatase, receptor type, M), RGS5 (regulator of G-protein signaling 5), and TUSC3 (tumor suppressor candidate 3), were also reported as TM expressed genes in three earlier non-microarray based studies.
RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation.
Lee et al., Taejŏn, South Korea. In Mol Biol Cell, 2011
differentiation into adipocytes is controlled by RPTPmu
Protein tyrosine phosphatase µ (PTP µ or PTPRM), a negative regulator of proliferation and invasion of breast cancer cells, is associated with disease prognosis.
Jiang et al., Cardiff, United Kingdom. In Plos One, 2011
BACKGROUND: PTPRM has been shown to exhibit homophilic binding and confer cell-cell adhesion in cells including epithelial and cancer cells.
Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.
Goldblum et al., Baltimore, United States. In Exp Lung Res, 2011
In A549 cells, diverse injurious stimuli dramatically reduced PTPmu protein expression.
Whole-exome sequencing uncovers frequent GNAS mutations in intraductal papillary mucinous neoplasms of the pancreas.
Shiratori et al., Tokyo, Japan. In Sci Rep, 2010
We performed whole-exome sequencing for a primary IPMN tissue, which uncovered somatic mutations in KCNF1, DYNC1H1, PGCP, STAB1, PTPRM, PRPF8, RNASE3, SPHKAP, MLXIPL, VPS13C, PRCC, GNAS, KRAS, RBM10, RNF43, DOCK2, and CENPF.
Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration.
Brady-Kalnay et al., Cleveland, United States. In Cancer Res, 2009
loss of cell surface PTPmu by proteolysis generates catalytically active PTPmu fragments that contribute to migration and survival of glioblastoma cells
Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
Jones et al., Oxford, United Kingdom. In Science, 2007
a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions is described
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