Your browser doesn't support javascript.
loading
Structural insights into membrane remodeling by SNX1.
Zhang, Yan; Pang, Xiaoyun; Li, Jian; Xu, Jiashu; Hsu, Victor W; Sun, Fei.
Afiliación
  • Zhang Y; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • 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.
  • Li J; Division of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115.
  • Xu J; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • 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.
  • 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.
Proc Natl Acad Sci U S A ; 118(10)2021 03 09.
Article en En | MEDLINE | ID: mdl-33658379
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.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Membrana Celular / Multimerización de Proteína / Nexinas de Clasificación Límite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2021 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Membrana Celular / Multimerización de Proteína / Nexinas de Clasificación Límite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2021 Tipo del documento: Article País de afiliación: China
...