PTPRM is a member of the protein tyrosine phosphatase family and can participate in a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPRM has been shown to mediate cell-cell aggregation through the interaction with another molecule of PTPRM on an adjacent cell. PTPRM can interact with scaffolding protein RACK1/GNB2L1 and this interaction may be necessary for downstream signaling in response to cell-cell adhesion. PTPRM has been shown to be expressed in human pulmonary vascular endothelia where it directly binds to VE-cadherin and regulates both the tyrosine phosphorylation state of VE-cadherin and barrier integrity.
The International journal of developmental biology, 47(5), 345-354 (2003-08-05)
The receptor-like protein tyrosine phosphatase mu (RPTPmu) belongs to the subfamily of meprin, A5, RPTPmu (MAM) domain-containing RPTPs, which are thought to play an important role in cell-cell adhesion mediated processes. The current study was designed to examine the expression
The Journal of biological chemistry, 281(8), 4903-4910 (2005-12-29)
The receptor protein-tyrosine phosphatase PTPmu is a member of the Ig superfamily of cell adhesion molecules. The extracellular domain of PTPmu contains motifs commonly found in cell adhesion molecules. The intracellular domain of PTPmu contains two conserved catalytic domains, only
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