A novel domain of caveolin-2 that controls nuclear targeting: regulation of insulin-specific ERK activation and nuclear translocation by caveolin-2.

ABSTRACT: Herein, we report that insulin-activated extracellular signal-regulated kinase (ERK) is translocated to the nuclear envelope by caveolin-2 (cav-2) and associates with lamin A/C in the inner nuclear membrane in response to insulin. We identified that the Ser¹⁵⁴ -Val¹⁵⁵ -Ser¹⁵⁶ domain on the C-terminal of cav-2 is essential for insulin-induced phosphorylation and nuclear targeting of ERK and cav-2. In human embryonic kidney 293T cells, ERK was not activated and translocated to the nucleus by insulin in comparison to insulin-like growth factor-1 (IGF-1). However, insulin-stimulated activation of ERK was induced by exogenous addition of cav-2. The activated ERK associated and translocated with the cav-2 to the nucleus. In turn, cav-2 promoted phospho-ERK interaction with lamin A/C in the inner

SUBMITTER: Kwon H 

PROVIDER: S-EPMC3922675 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature