Characterization of interaction between CLP36 and palladin

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

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2775-2785
Number of pages11
JournalFEBS Journal
Volume276
Issue number10
DOIs
Publication statusPublished - 05-2009
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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