Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1-Reference-Cited by-同舟云学术

Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1

Published:2020-10-02 Issue:40 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Soubias Olivier¹^ORCID,Pant Shashank²,Heinrich Frank³⁴^ORCID,Zhang Yue¹^ORCID,Roy Neeladri Sekhar⁵,Li Jess¹^ORCID,Jian Xiaoying⁵,Yohe Marielle E.⁶^ORCID,Randazzo Paul A.⁵^ORCID,Lösche Mathias³⁴⁷^ORCID,Tajkhorshid Emad²^ORCID,Byrd R. Andrew¹^ORCID

Affiliation:

1. Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA.

2. NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, Department of Biochemistry, Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

3. Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

4. NIST Center for Neutron Research, Gaithersburg, MD 20878, USA.

5. Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

6. Pediatric Oncology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

7. Department of Biomedical Engineering, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

Abstract

The ASAP1 PH domain binds to PIP 2 membranes, experiences conformational shifts, and recognizes Arf1 to initiate GTPase activity.

Funder

National Institutes of Health

U.S. Department of Commerce

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference57 articles.

1. Arf GTPases and their effectors: assembling multivalent membrane-binding platforms

2. Regulation of G protein‐coupled receptor signaling by plasma membrane organization and endocytosis

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5. Cellular and molecular interactions of phosphoinositides and peripheral proteins

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