Characterization of interaction between CLP36 and palladin

Masao Maeda, Eri Asano, Daisuke Ito, Satoko Ito, Yoshinori Hasegawa, Michinari Hamaguchi, Takeshi Senga

研究成果: Article査読

17 被引用数 (Scopus)

抄録

CLP36 is a member of the PDZ-LIM family of proteins, which associates with α-actinin and localizes to the actin cytoskeleton. CLP36 is involved in the formation of stress fibers and focal adhesions; however, the molecular mechanism of how CLP36 regulates stress fiber formation is still unknown. To investigate the physiological function of CLP36, we performed yeast two-hybrid screening, and found that CLP36 interacts with palladin. Palladin is an important structural element of the actin cytoskeleton that is ubiquitously expressed and associates with α-actinin. The interaction was dependent on the PDZ domain of CLP36 and the C-terminus of palladin, and silencing of palladin suppressed localization of CLP36 to stress fibers. Overexpression of the PDZ domain of CLP36 also inhibited the localization of palladin to stress fibers, suggesting that the association of CLP36 and palladin is important for the localization of both proteins to stress fibers. Our experimental results indicate that α-actinin, CLP36 and palladin form a protein complex and contribute to regulation of the actin cytoskeleton.

本文言語English
ページ(範囲)2775-2785
ページ数11
ジャーナルFEBS Journal
276
10
DOI
出版ステータスPublished - 05-2009
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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