Triple functional domain protein

Definition:

Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases. Involved in coordinating actin remodeling, which is necessary for cell migration and growth. Plays a key role in the regulation of neurite outgrowth and lamellipodia formation. In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (By similarity). May act as a regulator of adipogenesis (By similarity).

References:

[1]. A Debant, et al. 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. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5466-71. [Content Brief]

[2]. Katrin Deinhardt, et al. Neuronal growth cone retraction relies on proneurotrophin receptor signaling through Rac. Sci Signal. 2011 Dec 6;4(202):ra82. [Content Brief]

[3]. Reuben J Pengelly, et al. Mutations specific to the Rac-GEF domain of TRIO cause intellectual disability and microcephaly. J Med Genet. 2016 Nov;53(11):735-742. [Content Brief]

[4]. Sónia Barbosa, et al. Opposite Modulation of RAC1 by Mutations in TRIO Is Associated with Distinct, Domain-Specific Neurodevelopmental Disorders. Am J Hum Genet. 2020 Mar 5;106(3):338-355. [Content Brief]

[5]. K Seipel, et al. Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth. J Cell Sci. 1999 Jun;112 ( Pt 12):1825-34. [Content Brief]

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