Proteomics

Dataset Information

0

Raw data for mass spectrometry analysis of the effects of hypoxia on mitochondrial protein composition


ABSTRACT: This project wanted to demonstrate that mitoselfphagy degrades various mitochondrial proteins to a different extent. Therefore,we measured the levels of mitochondrial proteins under hypoxia by mass spectrometry analysis. After 24 hours of hypoxia, most mitochondrial proteins, locating at different mitochondrial compartments, were decreased to different extents relative to normoxic controls. After hypoxia, The certain mitochondrial proteins were increased, and some mitochondrial proteins remained almost unchanged. These data demonstrated that mitoselfphagy is different from traditional mitophagy that degrades the entire mitochondria, which degrades various mitochondrial proteins to a different extent.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Tianshu Hao  

LAB HEAD: Zhiyin Song

PROVIDER: PXD034375 | Pride | 2023-10-24

REPOSITORIES: Pride

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Publications

Hypoxia-reprogramed megamitochondrion contacts and engulfs lysosome to mediate mitochondrial self-digestion.

Hao Tianshu T   Yu Jianglong J   Wu Zhida Z   Jiang Jie J   Gong Longlong L   Wang Bingjun B   Guo Hanze H   Zhao Huabin H   Lu Bin B   Engelender Simone S   He He H   Song Zhiyin Z  

Nature communications 20230711 1


Mitochondria are the key organelles for sensing oxygen, which is consumed by oxidative phosphorylation to generate ATP. Lysosomes contain hydrolytic enzymes that degrade misfolded proteins and damaged organelles to maintain cellular homeostasis. Mitochondria physically and functionally interact with lysosomes to regulate cellular metabolism. However, the mode and biological functions of mitochondria-lysosome communication remain largely unknown. Here, we show that hypoxia remodels normal tubular  ...[more]

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