The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain (Q28144060)

1

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C Serra-Pagès

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E Iannotti

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K Seipel

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M Tang

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S P O'Brien

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M Streuli

Journal of Biological Chemistry

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language of work or name

English

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publication date

17 November 2000

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published in

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volume

275

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issue

46

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page(s)

36116-23

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cites work

The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains

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GAPs for rho-related GTPases

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Faciogenital dysplasia protein (FGD1) and Vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases

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The Rho GTPase and a putative RhoGEF mediate a signaling pathway for the cell shape changes in Drosophila gastrulation

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Trio combines with dock to regulate Pak activity during photoreceptor axon pathfinding in Drosophila

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The guanine nucleotide exchange factor trio mediates axonal development in the Drosophila embryo

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Dosage-sensitive, reciprocal genetic interactions between the Abl tyrosine kinase and the putative GEF trio reveal trio's role in axon pathfinding

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The Drosophila trio plays an essential role in patterning of axons by regulating their directional extension.

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Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins

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Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity

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C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases

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Identifiers

DOI

10.1074/JBC.M003775200

1 reference

Consolidated OpenCitations Corpus – April 2017

release_re6bdhf5nbchdksxik4f2e3lgm

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/re6bdhf5nbchdksxik4f2e3lgm

mapped directly with Wikidata item

24 November 2022

based on heuristic

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10948190

1 reference

Consolidated OpenCitations Corpus – April 2017