Homo-oligomerization Is Essential for F-actin Assembly by the Formin Family FH2 Domain
Open Access
- 1 November 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (48) , 50250-50256
- https://doi.org/10.1074/jbc.m404429200
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Actin Dynamics Control SRF Activity by Regulation of Its Coactivator MALCell, 2003
- Mechanism of Formin-Induced Nucleation of Actin FilamentsBiochemistry, 2002
- Mutant Actins Demonstrate a Role for Unpolymerized Actin in Control of Transcription by Serum Response FactorMolecular Biology of the Cell, 2002
- The Diaphanous-related Formin mDia1 Controls Serum Response Factor Activity through its Effects on Actin PolymerizationMolecular Biology of the Cell, 2002
- Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory DomainJournal of Biological Chemistry, 2001
- Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1Nature Cell Biology, 2000
- Rho Small G-Protein-Dependent Binding of mDia to an Src Homology 3 Domain-Containing IRSp53/BAIAP2Biochemical and Biophysical Research Communications, 2000
- Distinct Actions and Cooperative Roles of ROCK and mDia in Rho Small G Protein-induced Reorganization of the Actin Cytoskeleton in Madin–Darby Canine Kidney CellsMolecular Biology of the Cell, 1999
- Cooperation between mDia1 and ROCK in Rho-induced actin reorganizationNature Cell Biology, 1999
- p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilinThe EMBO Journal, 1997