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Cited by 62

The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.

Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth

Seipel, Katja, Medley, Quintus G., Kedersha, Nancy L., Zhang, Xin A., O’Brien, Stephen P., Serra-Pages, Carles, Hemler, Martin E., Streuli, Michel·1999·Journal of Cell Science
DOI 10.1242/jcs.112.12.1825
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Abstract

Rho family GTPases regulate diverse cellular processes, including extracellular signal-mediated actin cytoskeleton reorganization and cell growth. The functions of GTPases are positively regulated by guanine nucleotide exchange factors, which promote the exchange of GDP for GTP. Trio is a complex protein possessing two guanine nucleotide exchange factor domains, each with adjacent pleckstrin homology and SH3 domains, a protein serine/threonine kinase domain with an adjacent immunoglobulin-like domain and multiple spectrin-like domains. To assess the functional role of the two Trio guanine nucleotide exchange factor domains, NIH 3T3 cell lines stably expressing the individual guanine nucleotide exchange factor domains were established and characterized. Expression of the amino-terminal guanine nucleotide exchange factor domain results in prominent membrane ruffling, whereas cells expressing the carboxy-terminal guanine nucleotide exchange factor domain have lamellae that terminate in miniruffles. Moreover, cells expressing the amino-terminal guanine nucleotide exchange factor domain display more rapid cell spreading, haptotactic cell migration and anchorage-independent growth, suggesting that Trio regulates both cell motility and cell growth. Expression of full-length Trio in COS cells also alters actin cytoskeleton organization, as well as the distribution of focal contact sites. These findings support a role for Trio as a multifunctional protein that integrates and amplifies signals involved in coordinating actin remodeling, which is necessary for cell migration and growth.

Overview

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Registry

Crossref · 10.1242/jcs.112.12.1825

Cites

73 of 73 references verified0 citation errors · 0 not checkable

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Metadata

Authors
Seipel, K., Medley, Q. G., Kedersha, N. L., Zhang, X. A., O’Brien, S. P., Serra-Pages, C., Hemler, M. E., & Streuli, M.
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
1999-06-15
Volume
112
Issue
12
Pages
1825-1834
ISSN
  • 0021-9533
  • 1477-9137
DOI
10.1242/jcs.112.12.1825
Cited by
62
References
73
Language
en
Licence
www.biologists.com/user-licence-1-1/ (vor)

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.