The SH3 binding site in front of the WH1 domain contributes to the membrane binding of the BAR domain protein endophilin A2

Author:

Sim Pei Fang1,Chek Min Fey2,Nguyen Nhung Thi Hong1,Nishimura Tamako1,Inaba Takehiko1,Hakoshima Toshio2,Suetsugu Shiro134ORCID

Affiliation:

1. Nara Institute of Science and Technology Graduate School of Science and Technology, , 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

2. Nara Institute of Science and Technology Institute for Research Initiatives, , 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

3. Nara Institute of Science and Technology Data Science Center, , 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

4. Nara Institute of Science and Technology Center for Digital Green-innovation, , 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

Abstract

Abstract The Bin–Amphiphysin–Rvs (BAR) domain of endophilin binds to the cell membrane and shapes it into a tubular shape for endocytosis. Endophilin has a Src-homology 3 (SH3) domain at their C-terminal. The SH3 domain interacts with the proline-rich motif (PRM) that is found in proteins such as neural Wiskott–Aldrich syndrome protein (N-WASP). Here, we re-examined the binding sites of the SH3 domain of endophilin in N-WASP by machine learning-based prediction and identified the previously unrecognized binding site. In addition to the well-recognized PRM at the central proline-rich region, we found a PRM in front of the N-terminal WASP homology 1 (WH1) domain of N-WASP (NtPRM) as a binding site of the endophilin SH3 domain. Furthermore, the diameter of the membrane tubules in the presence of NtPRM mutant was narrower and wider than that in the presence of N-WASP and in its absence, respectively. Importantly, the NtPRM of N-WASP was involved in the membrane localization of endophilin A2 in cells. Therefore, the NtPRM contributes to the binding of endophilin to N-WASP in membrane remodeling.

Funder

JSPS

Japan Science and Technology Agency

Japan Society for the Promotion of Science

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3