Cooperation between mDia1 and ROCK in Rho-induced actin reorganization

Naoki Watanabe, Takayuki Kato, Akiko Fujita, Toshimasa Ishizaki, Shuh Narumiya

Research output: Contribution to journalArticlepeer-review

718 Citations (Scopus)


The small GTPase Rho induces the formation of actin stress fibres and mediates the formation of diverse actin structures. However, it remains unclear how Rho regulates its effectors to elicit such functions. Here we show that GTP-bound Rho activates its effector mDia1 by disrupting mDia1's intramolecular interactions. Active mDia1 induces the formation of thin actin stress fibres, which are disorganized in the absence of activity of the Rho-associated kinase ROCK. Moreover, active mDia1 transforms ROCK-induced condensed actin fibres into structures reminiscent of Rho-induced stress fibres. Thus mDia1 and ROCK work concurrently during Rho-induced stress-fibre formation. Intriguingly, mDia1 and ROCK, depending on the balance of the two activities, induce actin fibres of various thicknesses and densities. Thus Rho may induce the formation of different actin structures affected by the balance between mDia1 and ROCK signalling.

Original languageEnglish
Pages (from-to)136-143
Number of pages8
JournalNature cell biology
Issue number3
Publication statusPublished - 1999 Jul
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'Cooperation between mDia1 and ROCK in Rho-induced actin reorganization'. Together they form a unique fingerprint.

Cite this