Open AccessRASAL3 preferentially stimulates GTP hydrolysis of the Rho family small GTPase Rac2
Author(s) -
Yong Sun Shin,
Young Kook Kim,
Hye Min Kim,
Nakyoung Shin,
Tae Sung Kim,
Taeg Kyu Kwon,
Jang Hyun Choi,
Jong-Soo Chang
Publication year - 2018
Publication title -
biomedical reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.607
H-Index - 25
eISSN - 2049-9442
pISSN - 2049-9434
DOI - 10.3892/br.2018.1119
Subject(s) - gtpase , gtpase activating protein , rhoa , cdc42 , rac1 , microbiology and biotechnology , rac gtp binding proteins , ras superfamily , biology , signal transduction , guanine nucleotide exchange factor , gtp' , g protein , biochemistry , enzyme
Members of the Ras superfamily of small G-proteins serve as molecular switches of intracellular signaling pathways. Rac2 is a Rho subfamily GTPase switch that is specifically expressed in hematopoietic cells and regulates AKT activation in cell signaling. Ras activating protein-like 3 (RASAL3) is the recently identified Ras GTPase activating protein (GAP) that is also specifically expressed in hematopoietic cells and stimulates p21ras GTPase activity. The restricted expression of both Rac2 and RASAL3 suggests that they may serve critical roles in hematopoietic cell signaling. Here in the present study demonstrates that the catalytic domain of RASAL3 may also be able to interact with Rac2 and stimulate its GTPase activity in vitro . By contrast, p50 rhoGAP molecules did not markedly affect Rac2 GTPase activity, but did accelerate the activity of other Rho GTPases, including Rac1, RhoA and Cdc42. Collectively, the present results indicate, seemingly for the first time, that GAP activity for Rac2 is regulated by the RasGAP family protein, RASAL3.