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Low molecular weight phosphotyrosine protein phosphatase translocation during cell stimulation with platelet‐derived growth factor
Author(s) -
Rigacci Stefania,
Bucciantini Monica,
Marzocchini Riccardo,
Berti Andrea
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00847-3
Subject(s) - phosphorylation , platelet derived growth factor receptor , growth factor , phosphatase , stimulation , cytosol , receptor , microbiology and biotechnology , population , biology , chromosomal translocation , protein phosphatase 2 , biochemistry , enzyme , chemistry , endocrinology , medicine , gene , environmental health
Low M r phosphotyrosine protein phosphatase (PTP) is a cytosolic enzyme whose activity upon platelet‐derived growth factor (PDGF) and insulin receptors has been demonstrated in vivo. In our study we demonstrate that this enzyme, both naturally expressed and overexpressed in NIH/3T3 fibroblasts, translocates from the cytosol to the Triton X‐100 insoluble fraction following stimulation with PDGF. It emerges that the phosphorylation of a defined population of PDGF receptors, which is localized in this fraction and seems to be endowed with peculiar features and functions, is particularly affected by low M r PTP overexpression.