期刊
JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
卷 15, 期 4, 页码 888-908出版社
WILEY
DOI: 10.1111/j.1582-4934.2010.01079.x
关键词
caveolin-2; phospho-ERK; lamin A; C; nuclear translocation; insulin; IGF-1
资金
- Ministry for Health and Welfare, Republic of Korea [0920110]
- Ministry of Education, Science and Technology [2010-0007897]
- Korea Student Aid Foundation
- Gyeongsang National University
- Korea Health Promotion Institute [0920110] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2010-0007897, 전09A1117] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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 nuclear membrane. In contrast, ERK, but not cav-2, was phosphorylated and translocated to the nucleus by IGF-1. The nuclear targeted phospho-ERK failed to localize in the nuclear envelope in response to IGF-1. Together, our data demonstrate that translocation of phospho-ERK to the nuclear envelope is mediated by Ser154-Val155-Ser156 domain of cav-2 and this event is an insulin-specific action.
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