Evidence map›Paper›PMID 31291238›Full record

ArticlePLoS computational biology2019

ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.

Chun Chan, Xiaoyun Pang, Yan Zhang, Tongxin Niu, Shengjiang Yang, Daohui Zhao, Jian Li, Lanyuan Lu, Victor W Hsu, Jian Zhou and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PLoS computational biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Chun ChanDepartment of Materials Science and Engineering, City University of Hong Kong, Hong Kong, China.ORCID 0000-0002-3705-1835
Xiaoyun PangNational Laboratory of Biomacromolecules, CAS Center for excellence in biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-8476-3771
Yan ZhangNational Laboratory of Biomacromolecules, CAS Center for excellence in biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Tongxin NiuNational Laboratory of Biomacromolecules, CAS Center for excellence in biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Shengjiang YangSchool of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou, Guangdong, China.
Daohui ZhaoSchool of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou, Guangdong, China.
Jian LiDivision of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, Massachusetts, United States of America.
Lanyuan LuSchool of Biological Sciences, Nanyang Technological University, Singapore.
Victor W HsuDivision of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, Massachusetts, United States of America.
Jian ZhouSchool of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou, Guangdong, China.
Fei SunNational Laboratory of Biomacromolecules, CAS Center for excellence in biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Jun FanDepartment of Materials Science and Engineering, City University of Hong Kong, Hong Kong, China.ORCID 0000-0001-8227-9671

Funding

Mechanisms of Endocytic RecyclingR01GM115683 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HSU, VICTOR W · 2015 to 2018
$1.7M
NIGMS NIH HHS R01 GM115683
6 · The paper itself

Abstract

Studies on the Bin-Amphiphysin-Rvs (BAR) domain have advanced a fundamental understanding of how proteins deform membrane. We previously showed that a BAR domain in tandem with a Pleckstrin Homology (PH domain) underlies the assembly of ACAP1 (Arfgap with Coil-coil, Ankryin repeat, and PH domain I) into an unusual lattice structure that also uncovers a new paradigm for how a BAR protein deforms membrane. Here, we initially pursued computation-based refinement of the ACAP1 lattice to identify its critical protein contacts. Simulation studies then revealed how ACAP1, which dimerizes into a symmetrical structure in solution, is recruited asymmetrically to the membrane through dynamic behavior. We also pursued electron microscopy (EM)-based structural studies, which shed further insight into the dynamic nature of the ACAP1 lattice assembly. As ACAP1 is an unconventional BAR protein, our findings broaden the understanding of the mechanistic spectrum by which proteins assemble into higher-ordered structures to achieve membrane deformation.

Indexed as

Cell MembraneDimerizationGTPase-Activating ProteinsHumansMembrane ProteinsPleckstrin Homology DomainsProtein ConformationACAP1 protein, humanGTPase-Activating ProteinsMembrane Proteins

Identifiers

PMID31291238
PMCPMC6663034

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.