Proteomics analysis of autophagy-deficient Atg7−/− MEFs reveals a close relationship between F-actin and autophagy

•We identified 114 significantly altered proteins in Atg7−/− MEFs.•It included 48 up-regulated proteins and 66 down-regulated proteins.•F-actin was the center in the down-regulated protein network.•F-actin was loose and disassembled in the Atg7−/− MEFs.•Depolymerization of F-actin impaired autophago...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2013-08, Vol.437 (3), p.482-488
Main Authors: Zhuo, Cuiqin, Ji, Yuhua, Chen, Zhenping, Kitazato, Kaio, Xiang, Yangfei, Zhong, Meigong, Wang, Qiaoli, Pei, Ying, Ju, Huaiqiang, Wang, Yifei
Format: Article
Language:English
Subjects:
Actins - genetics
Actins - physiology
Animals
Atg7
Autophagy - genetics
Autophagy-deficient MEFs
Autophagy-Related Protein 7
Cell Line, Transformed
Cells, Cultured
Embryo, Mammalian - cytology
Embryo, Mammalian - metabolism
F-actin
Fibroblasts - cytology
Fibroblasts - metabolism
Mice
Microscopy, Confocal
Microtubule-Associated Proteins - deficiency
Microtubule-Associated Proteins - genetics
Phagosomes - metabolism
Phagosomes - pathology
Protein Interaction Maps - genetics
Proteomics - methods
Proteomics analysis
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Summary:•We identified 114 significantly altered proteins in Atg7−/− MEFs.•It included 48 up-regulated proteins and 66 down-regulated proteins.•F-actin was the center in the down-regulated protein network.•F-actin was loose and disassembled in the Atg7−/− MEFs.•Depolymerization of F-actin impaired autophagosome maturation in WT MEFs. Autophagy plays a crucial role in a wide array of physiological processes. To uncover the complex regulatory networks and mechanisms underlying basal autophagy, we performed a quantitative proteomics analysis of autophagy-deficient mouse embryonic fibroblast cells (MEFs) using iTRAQ labeling coupled with on-line 2D LC/MS/MS. We quantified a total of 1234 proteins and identified 114 proteins that were significantly altered (90% confidence interval), including 48 up-regulated proteins and 66 down-regulated proteins. We determined that F-actin was disassembled in autophagy-deficient Atg7−/− MEFs. Treatment of the WT MEFs with cytochalasin D (CD), which induces F-actin depolymerization, significantly induced autophagosome formation. However, treatment with cytochalasin D also increased the protein level of p62 under starvation conditions, suggesting that depolymerization of F-actin impaired autophagosome maturation and that the intact F-actin network is required for basal and starvation-induced autophagy. Our results demonstrate a close relationship between F-actin and autophagy and provide the basis for further investigation of their interactions.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2013.06.111