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Yeast TRAPPIII complex cross-linking mass spectrometry

ABSTRACT: A comprehensive analysis of the structure and function of the yeast TRAPPIII complex

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Kumar Yugandhar

LAB HEAD: Haiyuan Yu

PROVIDER: PXD025172 | Pride | 2021-06-02

REPOSITORIES: Pride

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Structural basis of TRAPPIII-mediated Rab1 activation.

Joiner Aaron Mn AM Phillips Ben P BP Yugandhar Kumar K Sanford Ethan J EJ Smolka Marcus B MB Yu Haiyuan H Miller Elizabeth A EA Fromme J Christopher JC

The EMBO journal 20210521 12

The GTPase Rab1 is a master regulator of the early secretory pathway and is critical for autophagy. Rab1 activation is controlled by its guanine nucleotide exchange factor, the multisubunit TRAPPIII complex. Here, we report the 3.7 Å cryo-EM structure of the Saccharomyces cerevisiae TRAPPIII complex bound to its substrate Rab1/Ypt1. The structure reveals the binding site for the Rab1/Ypt1 hypervariable domain, leading to a model for how the complex interacts with membranes during the activation ...[more]

PMID: 34018207

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