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Cited by 329

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Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory Domain

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Alberts, Arthur S.·2001·Journal of Biological Chemistry

Abstract

Mammalian and fungal Diaphanous-related formin homology (DRF) proteins contain several regions of conserved sequence homology. These include an amino-terminal GTPase binding domain (GBD) that interacts with activated Rho family members and formin homology domains that mediate targeting or interactions with signaling kinases and actin-binding proteins. DRFs also contain a conserved Dia-autoregulatory domain (DAD) in their carboxyl termini that binds the GBD. The GBD is a bifunctional autoinhibitory domain that is regulated by activated Rho. Expression of the isolated DAD in cells causes actin fiber formation and stimulates serum response factor-regulated gene expression. Inhibitor experiments show that the effects of exogenous DAD expression are dependent upon cellular Dia proteins. Alanine substitution of DAD consensus residues that disrupt GBD binding also eliminate DAD biological activity. Thus, DAD expression activates nuclear signaling and actin remodeling by mimicking activated Rho and unlatching the autoinhibited state of the cellular complement of Dia proteins.

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Metadata

Authors
Alberts, A. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-01
Volume
276
Issue
4
Pages
2824-2830
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2027866287
Cited by
329
References
40
FWCI
7.17
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory Domain. https://app.cochat.ai/papers/10.1074/jbc.m006205200
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Alberts, A. S. (2001). Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory Domain. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m006205200

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