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Whole cell proteome of DNAJC15 short, uncleavable and wild type overexpression

ABSTRACT: Mitochondria dynamically adapt to cellular stress to ensure cell survival. The stress-regulated mitochondrial peptidase OMA1 orchestrates these adaptive responses, which limit mitochondrial fusion and promote mitochondrial stress signaling and metabolic rewiring. Here, we show that cellular stress adaptation involves OMA1-mediated regulation of mitochondrial protein import and OXPHOS biogenesis. OMA1 cleaves the mitochondrial chaperone DNAJC15 and promotes its degradation by the m-AAA protease AFG3L2. Loss of DNAJC15 impairs mitochondrial protein import and restricts OXPHOS biogenesis under conditions of mitochondrial dysfunction. Non-imported mitochondrial preproteins accumulate at the endoplasmic reticulum inducing an unfolded protein response. Our results demonstrate stress-dependent changes in mitochondrial protein import as part of the OMA1-mediated mitochondrial stress response and highlight the interdependence of proteostasis regulation between different organelles.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Hendrik Nolte

LAB HEAD: Thomas Langer

PROVIDER: PXD072822 | Pride | 2026-01-20

REPOSITORIES: Pride

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			Action	DRS
	0170_SEARCH.zip	Other
	20211230_HN_0170_LaKr_sample_01.raw	Raw
	20211230_HN_0170_LaKr_sample_02.raw	Raw
	20211230_HN_0170_LaKr_sample_03.raw	Raw
	20211230_HN_0170_LaKr_sample_04_20220104100741.raw	Raw

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