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UVA inactivates protein tyrosine phosphatases by calpain‐mediated degradation
Author(s) -
Gulati Pawan,
Markova Boyka,
Göttlicher Martin,
Böhmer FrankD,
Herrlich Peter A
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400190
Subject(s) - protein tyrosine phosphatase , calpain , phosphatase , tyrosine , microbiology and biotechnology , chemistry , tyrosine kinase , receptor tyrosine kinase , biochemistry , degradation (telecommunications) , substrate (aquarium) , enzyme , phosphorylation , kinase , receptor , biology , telecommunications , computer science , ecology
UV irradiation causes inflammatory and proliferative cellular responses. We have proposed previously that these effects are, to a large extent, caused by the ligand‐independent activation of several receptor tyrosine kinases due to the inactivation of their negative control elements, the protein tyrosine phosphatases (PTPs). We examined the mechanism of this inactivation and found that, in addition to reversible oxidation of PTPs, UV triggers a novel mechanism: induced degradation of PTPs by calpain, which requires both calpain activation and substrate PTP oxidative modification. This as yet unrecognized effect of UV is irreversible, occurs predominantly with UVA and UVB, the range of wavelengths in sunlight that reach the skin surface, and at physiologically relevant doses.