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CROP: A Retromer- PROPPIN complex mediating membrane fission in the endo-lysosomal system

ABSTRACT: Endo-lysosomal compartments exchange proteins by fusing, fissioning, and through endosomal transport carriers. Thereby, they sort many plasma membrane receptors and transporters and control cellular signaling and metabolism. How the membrane fission events are catalyzed is poorly understood. Here, we identify the novel CROP complex as a factor acting at this step. CROP integrates PROPPIN Atg18 with a part of the endosome- and vacuole-associated retromer complex to generate a membrane fission device of much higher potency. We studied its activity in yeast, in human cells and on liposomes.

INSTRUMENT(S): LTQ Orbitrap Velos, Orbitrap Fusion, Q Exactive

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

SUBMITTER: Patrice Waridel

LAB HEAD: Andreas Mayer

PROVIDER: PXD031244 | Pride | 2022-05-05

REPOSITORIES: Pride

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CROP: a retromer-PROPPIN complex mediating membrane fission in the endo-lysosomal system.

Courtellemont Thibault T De Leo Maria Giovanna MG Gopaldass Navin N Mayer Andreas A

The EMBO journal 20220425 10

Endo-lysosomal compartments exchange proteins by fusing, fissioning, and through endosomal transport carriers. Thereby, they sort many plasma membrane receptors and transporters and control cellular signaling and metabolism. How the membrane fission events are catalyzed is poorly understood. Here, we identify the novel CROP complex as a factor acting at this step. CROP joins members of two protein families: the peripheral subunits of retromer, a coat forming endosomal transport carriers, and mem ...[more]

PMID: 35466426

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