Noncanonical Myo9b-RhoGAP Accelerates RhoA GTP Hydrolysis by a Dual-Arginine-Finger Mechanism
详细信息 查看全文
- 作者：Fengshuang Yi1 ; 5 ; &dagger ; ; Ruirui Kong2 ; &dagger ; ; Jinqi Ren1 ; &dagger ; ; Li Zhu2 ; Jizhong Lou3 ; Jane Y. Wu2 ; 4 ; jane-wu@northwestern.edu" class="auth_mail" title="E-mail the corresponding author ; Wei Feng1 ; wfeng@ibp.ac.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：GAPs ; GTPase-activating proteins ; RhoGAPs ; GAPs for Rho GTPases ; Myo9b ; Myosin IXb ; Myo9b-RhoGAP ; RhoGAP domain of Myo9b ; MD ; molecular dynamics ; GST ; glutathione S-transferase ; ITC ; isothermal titration calorimetry ; RBD ; rhotekin-binding domain ; DMEM ; Dulbecco's modified Eagle medium ; GST-RBD ; GST-fusion protein containing the RhoA-binding domain of rhotekin ; GST-PBD ; GST-fusion protein containing the Cdc42-binding domain of p21-activated kinase
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3043-3057
- 全文大小：1956 K
文摘
- class="listitem" id="list_l0005">
- class="label">•
The auxiliary asparagine of the canonical RhoGAP domains is missing in Myo9b-RhoGAP.
- class="label">•
The structure of the noncanonical Myo9b-RhoGAP/RhoA complex has been solved.
- class="label">•
Myo9b-RhoGAP contains two arginine fingers for accelerating RhoA GTP hydrolysis.
- class="label">•
Mutations of the two arginine fingers impair the catalytic activity of Myo9b-RhoGAP.
- class="label">•
The dual-arginine-finger mechanism expands the knowledge about RhoGAP catalysis.