Jul 16, 2013

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

Biochemical and Biophysical Research Communications
Cuiqin ZhuoYifei Wang

Abstract

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.

  • References21
  • Citations16

References

  • References21
  • Citations16

Citations

Mentioned in this Paper

Hepatitis D Infection
Autophagic Vacuole Maturation
Microtubule-Associated Protein 3
Isoactin
ATG7 gene
Macroautophagy
F-Actin
Autophagic Vacuole Assembly
Proteomics
Filamentous Actin Location

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