Proteomics

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E3 ligase regulates FAM134B ubiquitination

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: PXD032750 | Pride | 2023-06-19

REPOSITORIES: Pride

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Dataset's files

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20220119_UbSites_V1_FAM134B_WT_AFMR_V2_MUT_DMSO_1.raw Raw
20220119_UbSites_V1_FAM134B_WT_AFMR_V2_MUT_DMSO_2.raw Raw
20220119_UbSites_V1_FAM134B_WT_AFMR_V2_MUT_DMSO_3.raw Raw
20220119_UbSites_V1_FAM134B_WT_AFMR_V2_MUT_TOR_1.raw Raw
20220119_UbSites_V1_FAM134B_WT_AFMR_V2_MUT_TOR_2.raw Raw
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Publications

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]

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