Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation-Reference-Cited by-同舟云学术

Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation

Published:2022-02 Issue:6 Volume:119 Page:
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proc. Natl. Acad. Sci. U.S.A.

Author:

Klink Björn U.¹,Herrmann Eric²^ORCID,Antoni Claudia¹,Langemeyer Lars³^ORCID,Kiontke Stephan³^ORCID,Gatsogiannis Christos¹^ORCID,Ungermann Christian³⁴^ORCID,Raunser Stefan¹^ORCID,Kümmel Daniel²³^ORCID

Affiliation:

1. Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany

2. Institute of Biochemistry, University of Münster, 48149 Münster, Germany

3. Department of Biology/Chemistry, Osnabrück University, 49076 Osnabrück, Germany

4. Center of Cellular Nanoanalytics, Osnabrück University, 49076 Osnabrück, Germany

Abstract

Significance Rab GTPases are central regulators of intracellular trafficking and serve as markers of organelle identity. They act as molecular switches, and their activation requires precise spatiotemporal control. Members of the family of the Tri Longin domain (TLD) Rab-GEFs (guanine nucleotide exchange factors) act as activators of a subset of Rabs that play a critical role in late endosomal biogenesis. Genetic defects associated with TLD Rab-GEFs cause developmental diseases, but the underlying mechanisms are only partly understood. The determination of the structure of the TLD Rab-GEF Mon1-Ccz1 presented here provides a molecular basis for understanding the function and regulation of these proteins.

Funder

Deutsche Forschungsgemeinschaft

Max-Planck-Gesellschaft

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Link

https://pnas.org/doi/pdf/10.1073/pnas.2121494119

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