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The dephosphorylation characteristics of the receptors for epidermal growth factor and platelet‐derived growth factor in Swiss 3T3 cell membranes suggest differential regulation of receptor signalling by endogenous protein‐tyrosine phosphatases
Author(s) -
Böhmer Frank-D.,
Böhmer Sylvia-Annette,
Heldin Carl-Henrik
Publication year - 1993
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 - 10.1016/0014-5793(93)80352-u
Subject(s) - dephosphorylation , platelet derived growth factor receptor , epidermal growth factor , biology , growth factor receptor , microbiology and biotechnology , receptor tyrosine kinase , receptor , growth factor , phosphorylation , biochemistry , chemistry , phosphatase
Comparison of the phosphotyrosine‐specific dephosphorylation of the autophosphorylated receptors for epidermal growth factor (EGF) and platelet‐derived growth factor (PDGF) in Swiss 3T3 cell membranes by the endogenous phosphatases revealed striking differences. EGF receptor dephosphorylation was clearly faster than PDGF receptor dephosphorylation and strongly inhibited by Triton X‐100 and octylglucoside, whereas PDGF receptor dephosphorylation was to a lesser extent detergent‐susceptible. PDGF receptor dephosphorylation was effectively inhibited by phenylarsineoxide, protamine and poly‐lysine and partially by N ‐ethylmaleinimide, whereas EGF receptor dephosphorylation was not affected by these agents. We suggest that these differences in dephosphorylation of EGF and PDGF receptors are due to their differential interaction with membrane‐associated protein‐tyrosine phosphatases and important for differential regulation of receptor signalling.