RASAL3 preferentially stimulates GTP hydrolysis of the Rho family small GTPase Rac2

Shin,Yoonjae; Kim,Yong  Woo; Kim,Hyemin; Shin,Nakyoung; Kim,Tae  Sung; Kwon,Taeg  Kyu; Choi,Jang  Hyun; Chang,Jong-Soo

doi:10.3892/br.2018.1119

RASAL3 preferentially stimulates GTP hydrolysis of the Rho family small GTPase Rac2

Authors:
- Yoonjae Shin
- Yong Woo Kim
- Hyemin Kim
- Nakyoung Shin
- Tae Sung Kim
- Taeg Kyu Kwon
- Jang Hyun Choi
- Jong-Soo Chang
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Affiliations: Department of Life Science, College of Science and Technology, Daejin University, Pocheon-Si, Gyeonggi-Do 11159, South Korea, Department of Immunology and Physiology, School of Medicine, Keimyung University, Daegu 42601, South Korea, Department of Biological Sciences, Division of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 44919, South Korea
Published online on: July 2, 2018 https://doi.org/10.3892/br.2018.1119
Pages: 241-246

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Abstract

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.

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