Autophagy Induced by Calcium Phosphate Precipitates Involves Endoplasmic Reticulum Membranes in Autophagosome Biogenesis
| Autor: | Massaki Komatsu, Daohong Chen, Min Li, Xiao Ming Yin, Jun-Lin Guan, Xi Chen, Wentao Gao |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Calcium Phosphates
Autophagosome Immunoblotting ATG5 lcsh:Medicine chemistry.chemical_element Biology Calcium Endoplasmic Reticulum Biochemistry Signaling Pathways Cell Line 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Phagosomes Molecular Cell Biology Autophagy Calcium-Mediated Signal Transduction Humans Phosphatidylinositol Protein Interactions lcsh:Science Cellular Stress Responses 030304 developmental biology 0303 health sciences Multidisciplinary Cell Death Endoplasmic reticulum lcsh:R Proteins Cellular Structures Cell biology Subcellular Organelles nervous system chemistry 030220 oncology & carcinogenesis Autophagosome membrane Unfolded protein response Membranes and Sorting lcsh:Q psychological phenomena and processes Research Article Signal Transduction |
| Zdroj: | PLoS ONE, Vol 7, Iss 12, p e52347 (2012) PLoS ONE |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0052347 |
| Popis: | Calcium can play an important role in the regulation of autophagy. We previously reported that exogenously introduced calcium in the form of calcium phosphate precipitates (CPP) induces autophagy. Here we showed that CPP-induced autophagy required the classical autophagic machinery, including the autophagosome initiating molecules FIP200 and Beclin 1, as well as molecules involved in the autophagosome membrane extension, Atg4, Atg5 and Atg3. On the other hand, Atg9 seemed to place a restriction on CPP-induced autophagy. Loss of Atg9 led to enhanced LC3 punctation and enhanced p62 degradation. CPP-induced autophagy was independent of mTOR and reactive oxygen species. It also did not affect MAP kinase activation and ER stress. DFCP1 is an ER-resident molecule that binds to phosphatidylinositol 3-phosphate. CPP activated DFCP1 punctation in a class III phosphatidylinositol-3-kinase and calcium dependent manner, and caused the association of DFCP1 puncta with the autophagosomes. Consistently, ER membranes, but not Golgi or mitochondrial membranes, colocalized with CPP-induced LC3 positive autophagosomes. These data suggest that CPP-induced autophagosome formation involves the interaction with the ER membrane. |
| Databáze: | OpenAIRE |
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