論文

査読有り
2011年2月

WAVE2 Forms a Complex with PKA and Is Involved in PKA Enhancement of Membrane Protrusions

JOURNAL OF BIOLOGICAL CHEMISTRY
  • Hiroshi Yamashita
  • ,
  • Kazumitsu Ueda
  • ,
  • Noriyuki Kioka

286
5
開始ページ
3907
終了ページ
3914
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M110.145409
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

PKA contributes to many physiological processes, including glucose homeostasis and cell migration. The substrate specificity of PKA is low compared with other kinases; thus, complex formation with A-kinase-anchoring proteins is important for the localization of PKA in specific subcellular regions and the phosphorylation of specific substrates. Here, we show that PKA forms a complex with WAVE2 (Wiskott-Aldrich syndrome protein family verprolin-homologous protein 2) in MDA-MB-231 breast cancer cells and mouse brain extracts. Two separate regions of WAVE2 are involved in WAVE2-PKA complex formation. This complex localizes to the leading edge of MDA-MB-231 cells. PKA activation results in enlargement of the membrane protrusion. WAVE2 depletion impairs PKA localization at membrane protrusions and the enlargement of membrane protrusion induced by PKA activation. Together, these results suggest that WAVE2 works as an A-kinase-anchoring protein that recruits PKA at membrane protrusions and plays a role in the enlargement of membrane protrusions induced by PKA activation.

リンク情報
DOI
https://doi.org/10.1074/jbc.M110.145409
J-GLOBAL
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201102270674371168
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/21119216
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000286653200071&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M110.145409
  • ISSN : 0021-9258
  • J-Global ID : 201102270674371168
  • PubMed ID : 21119216
  • Web of Science ID : WOS:000286653200071

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