Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin

Hayeong Kwon, Kyuho Jeong, Eun Mi Hwang, Jae-Yong Park, Seong Geun Hong, Wan Sung Choi, Yunbae Pak

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The regulatory function of caveolin-2 in signal transducer and activator of transcription 3 (STAT3) signaling by insulin was investigated. Insulin-induced increase in phosphorylation of STAT3 was reduced by caveolin-2 siRNA. Mutagenesis studies identified that phosphorylation of tyrosines 19 and 27 on caveolin-2 is required for the STAT3 activation. Caveolin-2 Y27A mutation decreased insulin-induced phosphorylation of STAT3 interacting with caveolin-2. pY27-Caveolin-2 was required for nuclear translocation of pY705-STAT3 in response to insulin. In contrast, caveolin-2 Y19A mutation influenced neither the phosphorylation of STAT3 nor nuclear translocation of pY705-STAT3. pY19-Caveolin-2, however, was essential for insulin-induced DNA binding of pS727-STAT3 and STAT3-targeted gene induction in the nucleus. Finally, insulin-induced transcriptional activation of STAT3 depended on phosphorylation of both 19 and 27 tyrosines. Together, our data reveal that phosphotyrosine-caveolin-2 is a novel regulator for transcriptional activation of STAT3 in response to insulin.

Original languageEnglish
Pages (from-to)1325-1333
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1793
Issue number7
DOIs
Publication statusPublished - 2009 Jul 1
Externally publishedYes

Fingerprint

Caveolin 2
STAT3 Transcription Factor
Transcriptional Activation
Insulin
Phosphorylation
Tyrosine
Mutation
Phosphotyrosine
Mutagenesis
Small Interfering RNA

Keywords

  • Caveolin-2 siRNA
  • Caveolin-2 tyrosine variant mutant
  • Insulin
  • pS727-STAT3
  • pY19-Caveolin-2
  • pY27-Caveolin-2
  • pY705-STAT3
  • STAT3 transcriptional activation

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin. / Kwon, Hayeong; Jeong, Kyuho; Hwang, Eun Mi; Park, Jae-Yong; Hong, Seong Geun; Choi, Wan Sung; Pak, Yunbae.

In: Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1793, No. 7, 01.07.2009, p. 1325-1333.

Research output: Contribution to journalArticle

Kwon, Hayeong ; Jeong, Kyuho ; Hwang, Eun Mi ; Park, Jae-Yong ; Hong, Seong Geun ; Choi, Wan Sung ; Pak, Yunbae. / Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin. In: Biochimica et Biophysica Acta - Molecular Cell Research. 2009 ; Vol. 1793, No. 7. pp. 1325-1333.
@article{a94f34a9ebe1425a8f33d6f1c0f72d5e,
title = "Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin",
abstract = "The regulatory function of caveolin-2 in signal transducer and activator of transcription 3 (STAT3) signaling by insulin was investigated. Insulin-induced increase in phosphorylation of STAT3 was reduced by caveolin-2 siRNA. Mutagenesis studies identified that phosphorylation of tyrosines 19 and 27 on caveolin-2 is required for the STAT3 activation. Caveolin-2 Y27A mutation decreased insulin-induced phosphorylation of STAT3 interacting with caveolin-2. pY27-Caveolin-2 was required for nuclear translocation of pY705-STAT3 in response to insulin. In contrast, caveolin-2 Y19A mutation influenced neither the phosphorylation of STAT3 nor nuclear translocation of pY705-STAT3. pY19-Caveolin-2, however, was essential for insulin-induced DNA binding of pS727-STAT3 and STAT3-targeted gene induction in the nucleus. Finally, insulin-induced transcriptional activation of STAT3 depended on phosphorylation of both 19 and 27 tyrosines. Together, our data reveal that phosphotyrosine-caveolin-2 is a novel regulator for transcriptional activation of STAT3 in response to insulin.",
keywords = "Caveolin-2 siRNA, Caveolin-2 tyrosine variant mutant, Insulin, pS727-STAT3, pY19-Caveolin-2, pY27-Caveolin-2, pY705-STAT3, STAT3 transcriptional activation",
author = "Hayeong Kwon and Kyuho Jeong and Hwang, {Eun Mi} and Jae-Yong Park and Hong, {Seong Geun} and Choi, {Wan Sung} and Yunbae Pak",
year = "2009",
month = "7",
day = "1",
doi = "10.1016/j.bbamcr.2009.04.015",
language = "English",
volume = "1793",
pages = "1325--1333",
journal = "Biochimica et Biophysica Acta - Molecular Cell Research",
issn = "0167-4889",
publisher = "Elsevier",
number = "7",

}

TY - JOUR

T1 - Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin

AU - Kwon, Hayeong

AU - Jeong, Kyuho

AU - Hwang, Eun Mi

AU - Park, Jae-Yong

AU - Hong, Seong Geun

AU - Choi, Wan Sung

AU - Pak, Yunbae

PY - 2009/7/1

Y1 - 2009/7/1

N2 - The regulatory function of caveolin-2 in signal transducer and activator of transcription 3 (STAT3) signaling by insulin was investigated. Insulin-induced increase in phosphorylation of STAT3 was reduced by caveolin-2 siRNA. Mutagenesis studies identified that phosphorylation of tyrosines 19 and 27 on caveolin-2 is required for the STAT3 activation. Caveolin-2 Y27A mutation decreased insulin-induced phosphorylation of STAT3 interacting with caveolin-2. pY27-Caveolin-2 was required for nuclear translocation of pY705-STAT3 in response to insulin. In contrast, caveolin-2 Y19A mutation influenced neither the phosphorylation of STAT3 nor nuclear translocation of pY705-STAT3. pY19-Caveolin-2, however, was essential for insulin-induced DNA binding of pS727-STAT3 and STAT3-targeted gene induction in the nucleus. Finally, insulin-induced transcriptional activation of STAT3 depended on phosphorylation of both 19 and 27 tyrosines. Together, our data reveal that phosphotyrosine-caveolin-2 is a novel regulator for transcriptional activation of STAT3 in response to insulin.

AB - The regulatory function of caveolin-2 in signal transducer and activator of transcription 3 (STAT3) signaling by insulin was investigated. Insulin-induced increase in phosphorylation of STAT3 was reduced by caveolin-2 siRNA. Mutagenesis studies identified that phosphorylation of tyrosines 19 and 27 on caveolin-2 is required for the STAT3 activation. Caveolin-2 Y27A mutation decreased insulin-induced phosphorylation of STAT3 interacting with caveolin-2. pY27-Caveolin-2 was required for nuclear translocation of pY705-STAT3 in response to insulin. In contrast, caveolin-2 Y19A mutation influenced neither the phosphorylation of STAT3 nor nuclear translocation of pY705-STAT3. pY19-Caveolin-2, however, was essential for insulin-induced DNA binding of pS727-STAT3 and STAT3-targeted gene induction in the nucleus. Finally, insulin-induced transcriptional activation of STAT3 depended on phosphorylation of both 19 and 27 tyrosines. Together, our data reveal that phosphotyrosine-caveolin-2 is a novel regulator for transcriptional activation of STAT3 in response to insulin.

KW - Caveolin-2 siRNA

KW - Caveolin-2 tyrosine variant mutant

KW - Insulin

KW - pS727-STAT3

KW - pY19-Caveolin-2

KW - pY27-Caveolin-2

KW - pY705-STAT3

KW - STAT3 transcriptional activation

UR - http://www.scopus.com/inward/record.url?scp=67649397307&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67649397307&partnerID=8YFLogxK

U2 - 10.1016/j.bbamcr.2009.04.015

DO - 10.1016/j.bbamcr.2009.04.015

M3 - Article

C2 - 19427337

AN - SCOPUS:67649397307

VL - 1793

SP - 1325

EP - 1333

JO - Biochimica et Biophysica Acta - Molecular Cell Research

JF - Biochimica et Biophysica Acta - Molecular Cell Research

SN - 0167-4889

IS - 7

ER -