c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14.

Article Details

Citation

Sanguinetti AR, Mastick CC

c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14.

Cell Signal. 2003 Mar;15(3):289-98.

PubMed ID
12531427 [ View in PubMed
]
Abstract

Caveolin-1 is phosphorylated at tyrosine 14 in response to cellular stress. Tyrosine 14 is a consensus Abl phosphorylation site suggesting that caveolin-1 may be an Abl substrate. We report here that expression of c-Abl is required for oxidative stress-induced caveolin-1 phosphorylation. In contrast, c-Src expression is not required. Phosphocaveolin is one of only two phosphotyrosine signals missing in lysates from the Abl(-/-) cells, indicating that these cells still respond to oxidative stress. Oxidative stress-induced tyrosine phosphorylation of caveolin-1 occurs only at the Abl site, tyrosine 14. Caveolin-1 is also a major phosphotyrosine signal detected in cells over-expressing c-Abl. Our results show that Abl activation leads to phosphorylation of caveolin-1 on tyrosine 14. Both Abl and caveolin have been linked to the actin cytoskeleton, and oxidative stress-induced phosphocaveolin is enriched at focal contacts. This suggests that phosphocaveolin regulates these structures, perhaps through recruiting and activating SH2-domain proteins such as Csk.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Tyrosine-protein kinase ABL1P00519Details