Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole-Reference-Cited by-同舟云学术

Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole

Published:2021-12-01 Issue:22 Volume:32 Page:
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

González Montoro Ayelén¹²,Vargas Duarte Prado³,Auffarth Kathrin³,Walter Stefan²,Fröhlich Florian⁴²,Ungermann Christian³²

Affiliation:

1. Cellular Communication Laboratory, Osnabrück University, 49076 Osnabrück, Germany

2. Center of Cellular Nanoanalytic Osnabrück (CellNanOs), Osnabrück University, 49076 Osnabrück, Germany

3. Biochemistry section, Osnabrück University, 49076 Osnabrück, Germany

4. Molecular Membrane Biology section, Department of Biology/Chemistry, Osnabrück University, 49076 Osnabrück, Germany

Abstract

The HOPS subunit Vps39 can participate in other functions such as vCLAMP formation, while the remaining subcomplex is available for its function in tethering and fusion.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference52 articles.

1. The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

2. Cryo-EM Structure of the TOM Core Complex from Neurospora crassa

3. Competitive organelle-specific adaptors recruit Vps13 to membrane contact sites

4. Preprotein Translocase of the Outer Mitochondrial Membrane: Reconstituted Tom40 Forms a Characteristic TOM Pore

5. The Vam6 GEF Controls TORC1 by Activating the EGO Complex

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