Regulation of cross-linking of actin filament by IQGAP1, a target for Cdc42

Masaki Fukataf, Shinya Kuroda, Katsuhiko Fujii, Tomoko Nakamura, Ikuo Shoji, Yoshiharu Matsuura, Katsuya Okawa, Akihiro Iwamatsu, Akira Kikuchi, Kozo Kaibuchi

研究成果: Article査読

163 被引用数 (Scopus)

抄録

We have previously shown that IQGAP1, a recently identified target for Cdc42 and Rac1 small GTPases, showed a distribution similar to that of cortical actin cytoskeleton at the membrane ruffling area induced by insulin and Rac1(val12) (Kuroda, S., Fukata, M., Kobayashi, K., Nakafuku, M., Nomura, N., Iwamatsu, A., and Kaibuchi, K. (1996) J. Biol. Chem. 271, 23363-23367). Here we identified an IQGAP1-interacting molecule with molecular mass of 43 kDa (p43) from bovine brain cytosol, using glutathione S-transferase (GST)- IQGAP1 affinity column chromatography. The amine acid sequencing of the protein revealed that p43 was identical to β- and γ-actin. IQGAP1 was cosedimentated with filamentous actin (F-actin). The amino-terminal domain (amino acids 1-216) of IQGAP1 was responsible for the interaction with F- actin. Falling ball viscometry assay revealed that IQGAP1 cross-linked the F- actin. This IQGAP1 activity was further enhanced by guanosine 5'-(3-0- thio)triphosphate (GTPγS)-GST-Cdc42 but not by GDP-GST-Cdc42. The gel filtration analysis of IQGAP1 revealed that IQGAP1 appeared as oligomers and that GTPγS-GST-Cdc42 but not GDP-GST-Cdc42 enhanced the oligomerization of IQGAP1. These results strongly suggest that IQGAP1, acting downstream of Cdc42, can cross-link the actin filament through its oligomerization.

本文言語English
ページ(範囲)29579-29583
ページ数5
ジャーナルJournal of Biological Chemistry
272
47
DOI
出版ステータスPublished - 21-11-1997
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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