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Dbl family guanine nucleotide exchange factors
Abstract
The Dbl family of guanine nucleotide exchange factors are multifunctional molecules that transduce diverse intracellular signals leading to the activation of Rho GTPases. The tandem Dbl-homology and pleckstrin-homology domains shared by all members of this family represent the structural module responsible for catalyzing the GDP-GTP exchange reaction of Rho proteins. Recent progress in genomic, genetic, structural and biochemical studies has implicated Dbl family members in diverse biological processes, including growth and development, skeletal muscle formation, neuronal axon guidance and tissue organization. The detailed pictures of their autoregulation, agonist-controlled activation and mechanism of interaction with Rho GTPase substrates, have begun to emerge.
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“The cycling of Rho GTPases between GTP-bound, active and guanosine diphosphate–bound, inactive forms is regulated by distinct cellular proteins including guanine nucleotide exchange factors and GTPase activating proteins (GAPs).2,3”
From Cross-talk between RhoH and Rac1 in regulation of actin cytoskeleton and chemotaxis of hematopoietic progenitor cells (2008) · cites this paper as [3]
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Gao, Y., Xing, J., Streuli, M., Leto, T. L., & Zheng, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108865200 · Cited by 115
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Trp56 of Rac1 Specifies Interaction with a Subset of Guanine Nucleotide Exchange Factors
Gao, Y., Xing, J., Streuli, M., Leto, T. L., & Zheng, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108865200 · Cited by 115
Self-citationDeciphering the Molecular and Functional Basis of Dbl Family Proteins
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Metadata
- Authors
- Zheng, Y.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2001-12
- Volume
- 26
- Issue
- 12
- Pages
- 724-732
- ISSN
- 0968-0004
- Cited by
- 339
- References
- 3
- Language
- en
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