The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory Domain
Open accessAbstract
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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Cites
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Autoinhibition and activation mechanisms of the Wiskott–Aldrich syndrome protein
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Signal-Regulated Activation of Serum Response Factor Is Mediated by Changes in Actin Dynamics
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Cell Wall Integrity Signaling in Saccharomyces cerevisiae
Levin, D. E. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.2.262-291.2005 · Cited by 1,136
Habas, R., Kato, Y., & He, X. (2001) · Cell · doi:10.1016/s0092-8674(01)00614-6 · Cited by 842
ROCK and Dia have opposing effects on adherens junctions downstream of Rho
Sahai, E., & Marshall, C. J. (2002) · Nature Cell Biology · doi:10.1038/ncb796 · Cited by 466
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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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