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ER-phagy regulates ER dynamics during myogenesis (3)

ABSTRACT: Proteomic landscape of primary murine myoblasts and differentiated myotubes

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Paolo Grumati

LAB HEAD: Paolo Grumati

PROVIDER: PXD050893 | Pride | 2024-12-27

REPOSITORIES: pride

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			Action	DRS
	2022-6-24_MS_PG_mMyoblasts_D0_1.raw	Raw
	2022-6-24_MS_PG_mMyoblasts_D0_2.raw	Raw
	2022-6-24_MS_PG_mMyoblasts_D0_3.raw	Raw
	2022-6-24_MS_PG_mMyoblasts_D10DM_1.raw	Raw
	2022-6-24_MS_PG_mMyoblasts_D10DM_2.raw	Raw

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ER-phagy regulates ER dynamics during myogenesis (1)

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Fam134c and Fam134b shape axonal endoplasmic reticulum architecture in vivo.

Project description:Endoplasmic reticulum (ER) remodeling is vital for cellular organization. ER-phagy, a selective autophagy targeting ER, plays an important role in maintaining ER morphology and function. The FAM134 protein family, including FAM134A, FAM134B, and FAM134C, mediates ER-phagy. While FAM134B mutations are linked to hereditary sensory and autonomic neuropathy in humans, the physiological role of the other FAM134 proteins remains unknown. To address this, we investigated the roles of FAM134 proteins using single and combined knockouts (KOs) in mice. Single KO in young mice showed no major phenotypes, however, combined Fam134b and Fam134c deletion (Fam134b/cdKO), but not the combination including Fam134a deletion, led to rapid neuromuscular and somatosensory degeneration, resulting in premature death. Fam134b/cdKO mice show rapid loss of motor and sensory axons in the peripheral nervous system. Long axons from Fam134b/cdKO mice exhibited expanded tubular ER with a transverse ladder-like appearance, whereas no obvious abnormalities were observed in cortical ER. Our study unveils critical roles of FAM134C and FAM134B in the formation of tubular ER network in axons of both motor and sensory neurons.

2024-06-24 | PXD050983 | Pride

Critical functions of FAM134 family members in endoplasmic reticulum remodeling, ER-phagy and collagen quality control

Project description:Degradation of the endoplasmic reticulum (ER) by selective autophagy (ER-phagy) is vital for cellular homeostasis. Here, we introduce FAM134A/RETREG2 and FAM134C/RETREG3 as new ER-phagy receptors. FAM134A and FAM134C exist in a relatively inactive state under basal conditions and require an activation signal to induce significant ER fragmentation. Molecular modeling and simulations implicate a single compact fold of FAM134A’s reticulon homology domain (RHD). In contrast, the RHDs of FAM134B and FAM134C are able to adopt at least three discrete conformations. These differences result in slower vesicle formation for FAM134A compared to FAM134C and mostly FAM134B. Global proteomic analyses of knockout MEFs indicate both distinct and overlapping roles for the Fam134s, with Fam134a being most distant from Fam134b and Fam134c. Fam134c appears to enhance and facilitate Fam134b’s role in maintaining pro-collagen-I levels and is therefore insufficient to compensate for its loss. By contrast, Fam134a has a particular mode of action in maintaining pro-collagen-I levels and is able to fully compensate loss of Fam134b or Fam134c upon over-expression in its wild-type or LIR mutant form.

2021-06-23 | PXD025626 | Pride

ER-phagy regulates ER dynamics during myogenesis

Project description:Endoplasmic reticulum (ER) plasticity and ER-phagy are intertwined processes essential for maintaining ER dynamics. We investigated the interplay between two isoforms of the ER-phagy receptor FAM134B in regulating ER remodeling in differentiating myoblasts. During myogenesis, the canonical FAM134B1 is degraded, while its isoform FAM134B2 is transcriptionally upregulated. The switch, favoring FAM134B2, indicates its significance as a regulator of ER morphology during myogenesis. FAM134B2 partial reticulon homology domain, with its rigid conformational characteristics, enables an efficient ER reshaping. FAM134B2 action increases in the active phase of differentiation leading to ER restructuring via ER-phagy, which then reverts to physiological levels when myotubes are mature and the ER reorganized. Knocking out both FAM134B isoforms in myotubes results in aberrant proteome landscape and the formation of dilated ER structures, both of which are rescued by FAM134B2 re-expression. Our results underscore how the fine tuning of FAM134B isoforms and ER-phagy orchestrate the ER dynamics during myogenesis providing insights into the molecular mechanisms governing ER homeostasis in muscle cells.

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