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FAM134B oligomer ubiquitination and ER-phagy

ABSTRACT: FAM134B is a reticulon-homology domain (RHD)-containing protein that participates in membrane-shaping of the endoplasmic reticulum (ER)8 13. It also functions as a mammalian ER-phagy receptor, mediating the fragmentation and selective degradation of ER sheets in multiple cell types8. However, little is known about the molecular and biophysical mechanisms that control and/or switch between these two FAM134B functions.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Adriana Covarrubias-Pinto

LAB HEAD: Ivan Dikic

PROVIDER: PXD032741 | Pride | 2023-06-19

REPOSITORIES: Pride

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Ubiquitination regulates ER-phagy and remodelling of endoplasmic reticulum.

González Alexis A Covarrubias-Pinto Adriana A Bhaskara Ramachandra M RM Glogger Marius M Kuncha Santosh K SK Xavier Audrey A Seemann Eric E Misra Mohit M Hoffmann Marina E ME Bräuning Bastian B Balakrishnan Ashwin A Qualmann Britta B Dötsch Volker V Schulman Brenda A BA Kessels Michael M MM Hübner Christian A CA Heilemann Mike M Hummer Gerhard G Dikić Ivan I

Nature 20230524 7964

The endoplasmic reticulum (ER) undergoes continuous remodelling via a selective autophagy pathway, known as ER-phagy<sup>1</sup>. ER-phagy receptors have a central role in this process<sup>2</sup>, but the regulatory mechanism remains largely unknown. Here we report that ubiquitination of the ER-phagy receptor FAM134B within its reticulon homology domain (RHD) promotes receptor clustering and binding to lipidated LC3B, thereby stimulating ER-phagy. Molecular dynamics (MD) simulations showed how ...[more]

PMID: 37225996

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E3 ligase regulates FAM134B ubiquitination

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ARL6IP1 is an interacting partner of the ER-phagy receptor FAM134B

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