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Conformation of the AP-3 complex explains its role in cargo recruitment at the Golgi

ABSTRACT: Crosslinking mass spectrometry study of an important adapter protein complex at the Golgi AP-3. We performed crosslinking mass spectrometry study using crosslinker DSSO and analyzed the digested peptides by LC-MS. The crosslinking study provided important information the subunit connectivity of AP-3, which facilitated the structural analysis of AP-3 by cyro-EM.

INSTRUMENT(S): Orbitrap Fusion Lumos

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

SUBMITTER: Heike Stephanowitz

LAB HEAD: Christian Ungermann

PROVIDER: PXD028005 | Pride | 2022-02-17

REPOSITORIES: Pride

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Flexible open conformation of the AP-3 complex explains its role in cargo recruitment at the Golgi.

Schoppe Jannis J Schubert Evelyn E Apelbaum Amir A Yavavli Erdal E Birkholz Oliver O Stephanowitz Heike H Han Yaping Y Perz Angela A Hofnagel Oliver O Liu Fan F Piehler Jacob J Raunser Stefan S Ungermann Christian C

The Journal of biological chemistry 20211022 5

Vesicle formation at endomembranes requires the selective concentration of cargo by coat proteins. Conserved adapter protein complexes at the Golgi (AP-3), the endosome (AP-1), or the plasma membrane (AP-2) with their conserved core domain and flexible ear domains mediate this function. These complexes also rely on the small GTPase Arf1 and/or specific phosphoinositides for membrane binding. The structural details that influence these processes, however, are still poorly understood. Here we pres ...[more]

PMID: 34688652

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Flexible open conformation of the AP-3 complex explains its role in cargo recruitment at the Golgi.

Project description: Not available

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