Journal
AUTOPHAGY
Volume 16, Issue 12, Pages 2219-2237Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2020.1719746
Keywords
ATG5; CALCOCO1; MAP1LC3; mass spectrometry proteomics; MTOR; reticulophagy; selective autophagy; ULK1; ULK2
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Funding
- Ride Cincinnati Foundation
- National Institute of General Medical Sciences [1R35GM131795]
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Macroautophagy/autophagy is suppressed by MTOR (mechanistic target of rapamycin kinase) and is an anticancer target under active investigation. Yet, MTOR-regulated autophagy remains incompletely mapped. We used proteomic profiling to identify proteins in the MTOR-autophagy axis. Wild-type (WT) mouse cell lines and cell lines lacking individual autophagy genes (Atg5 or Ulk1/Ulk2) were treated with an MTOR inhibitor to induce autophagy and cultured in media with either glucose or galactose. Mass spectrometry proteome profiling revealed an elevation of known autophagy proteins and candidates for new autophagy components, including CALCOCO1 (calcium binding and coiled-coil domain protein 1). We show that CALCOCO1 physically interacts with MAP1LC3C, a key protein in the machinery of autophagy. Genetic deletion of CALCOCO1 disrupted autophagy of the endoplasmic reticulum (reticulophagy). Together, these results reveal a role for CALCOCO1 in MTOR-regulated selective autophagy. More generally, the resource generated by this work provides a foundation for establishing links between the MTOR-autophagy axis and proteins not previously linked to this pathway.
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