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 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 language | English |
|---|---|
| Pages (from-to) | 888-908 |
| Number of pages | 21 |
| Journal | Journal of Cellular and Molecular Medicine |
| Volume | 15 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2011 Apr 1 |
| Externally published | Yes |
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Keywords
- Caveolin-2
- IGF-1
- Insulin
- Lamin A/C
- Nuclear translocation
- Phospho-ERK
ASJC Scopus subject areas
- Molecular Medicine
- Cell Biology
Cite this
A novel domain of caveolin-2 that controls nuclear targeting : Regulation of insulin-specific ERK activation and nuclear translocation by caveolin-2. / Kwon, Hayeong; Jeong, Kyuho; Hwang, Eun Mi; Park, Jae-Yong; Pak, Yunbae.
In: Journal of Cellular and Molecular Medicine, Vol. 15, No. 4, 01.04.2011, p. 888-908.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A novel domain of caveolin-2 that controls nuclear targeting
T2 - Regulation of insulin-specific ERK activation and nuclear translocation by caveolin-2
AU - Kwon, Hayeong
AU - Jeong, Kyuho
AU - Hwang, Eun Mi
AU - Park, Jae-Yong
AU - Pak, Yunbae
PY - 2011/4/1
Y1 - 2011/4/1
N2 - 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.
AB - 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.
KW - Caveolin-2
KW - IGF-1
KW - Insulin
KW - Lamin A/C
KW - Nuclear translocation
KW - Phospho-ERK
UR - http://www.scopus.com/inward/record.url?scp=79954995335&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79954995335&partnerID=8YFLogxK
U2 - 10.1111/j.1582-4934.2010.01079.x
DO - 10.1111/j.1582-4934.2010.01079.x
M3 - Article
VL - 15
SP - 888
EP - 908
JO - Journal of Cellular and Molecular Medicine
JF - Journal of Cellular and Molecular Medicine
SN - 1582-1838
IS - 4
ER -