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

Hayeong Kwon, Kyuho Jeong, Eun Mi Hwang, Jae-Yong Park, Yunbae Pak

Research output: Contribution to journalArticle

17 Citations (Scopus)


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 Ser 154 -Val 155 -Ser 156 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 Ser 154 -Val 155 -Ser 156 domain of cav-2 and this event is an insulin-specific action.

Original languageEnglish
Pages (from-to)888-908
Number of pages21
JournalJournal of Cellular and Molecular Medicine
Issue number4
Publication statusPublished - 2011 Apr 1
Externally publishedYes



  • Caveolin-2
  • IGF-1
  • Insulin
  • Lamin A/C
  • Nuclear translocation
  • Phospho-ERK

ASJC Scopus subject areas

  • Molecular Medicine
  • Cell Biology

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