Structural insights into membrane remodeling by SNX1.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
09 03 2021
Historique:
entrez: 4 3 2021
pubmed: 5 3 2021
medline: 17 8 2021
Statut: ppublish

Résumé

The sorting nexin (SNX) family of proteins deform the membrane to generate transport carriers in endosomal pathways. Here, we elucidate how a prototypic member, SNX1, acts in this process. Performing cryoelectron microscopy, we find that SNX1 assembles into a protein lattice that consists of helical rows of SNX1 dimers wrapped around tubular membranes in a crosslinked fashion. We also visualize the details of this structure, which provides a molecular understanding of how various parts of SNX1 contribute to its ability to deform the membrane. Moreover, we have compared the SNX1 structure with a previously elucidated structure of an endosomal coat complex formed by retromer coupled to a SNX, which reveals how the molecular organization of the SNX in this coat complex is affected by retromer. The comparison also suggests insight into intermediary stages of assembly that results in the formation of the retromer-SNX coat complex on the membrane.

Identifiants

pubmed: 33658379
pii: 2022614118
doi: 10.1073/pnas.2022614118
pmc: PMC7958236
pii:
doi:

Substances chimiques

SNX1 protein, mouse 0
Sorting Nexins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM058615
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM115683
Pays : United States
Organisme : NIGMS NIH HHS
ID : R37 GM058615
Pays : United States

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Yan Zhang (Y)

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Xiaoyun Pang (X)

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; pangxy@moon.ibp.ac.cn vhsu@bwh.harvard.edu feisun@ibp.ac.cn.

Jian Li (J)

Division of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115.

Jiashu Xu (J)

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Victor W Hsu (VW)

Division of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115; pangxy@moon.ibp.ac.cn vhsu@bwh.harvard.edu feisun@ibp.ac.cn.

Fei Sun (F)

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; pangxy@moon.ibp.ac.cn vhsu@bwh.harvard.edu feisun@ibp.ac.cn.
School of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China.
Center for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

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Classifications MeSH