TCL is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rho family of GTPases.[1][2]
TCL (TC10-like) shares 85% and 78% amino acid similarity to TC10 and Cdc42, respectively. TCL mRNA is 2.5 kb long and is mainly expressed in heart. In vitro, TCL shows rapid GDP/GTP exchange and displays higher GTP dissociation and hydrolysis rates than TC10. Like other Rac/Cdc42/RhoUV members, GTP-bound TCL interacts with CRIB domains, such as those found in PAK and WASP. TCL produces large and dynamic F-actin-rich ruffles on the dorsal cell membrane in REF-52 fibroblasts. TCL activity is blocked by dominant negative Rac1 and Cdc42 mutants, suggesting a cross-talk between these three Rho GTPases.[3]
TCL is unrelated to TCL1A, a proto-oncogene implicated in the development of T-Cell Leukemias.
See also
editReferences
edit- ^ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
- ^ Boureux A, Vignal E, Faure S, Fort P (2007). "Evolution of the Rho family of ras-like GTPases in eukaryotes". Mol Biol Evol. 24 (1): 203–16. doi:10.1093/molbev/msl145. ISSN 0021-9193. PMC 2665304. PMID 17035353.
- ^ Vignal E, De Toledo M, Comunale F, Ladopoulou A, Gauthier-Rouviere C, Blangy A, Fort P (2007). "Characterization of TCL, a new GTPase of the rho family related to TC10 and Ccdc42". J Biol Chem. 275 (46): 36457–64. doi:10.1074/jbc.M003487200. ISSN 0021-9258. PMID 10967094.
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