Cited by 99Autophagy in Disease and TherapyCellular transport and secretionFungal and yeast genetics research

Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagy

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Nazarko, Taras Y., Ozeki, Katharine, Till, Andreas, Ramakrishnan, Geetha, Lotfi, Pouya, Yan, Mingda, Subramani, Suresh·2014·Journal of Cell Biology

Abstract

Autophagy is a membrane trafficking pathway that sequesters proteins and organelles into autophagosomes. The selectivity of this pathway is determined by autophagy receptors, such as the Pichia pastoris autophagy-related protein 30 (Atg30), which controls the selective autophagy of peroxisomes (pexophagy) through the assembly of a receptor protein complex (RPC). However, how the pexophagic RPC is regulated for efficient formation of the phagophore, an isolation membrane that sequesters the peroxisome from the cytosol, is unknown. Here we describe a new, conserved acyl-CoA–binding protein, Atg37, that is an integral peroxisomal membrane protein required specifically for pexophagy at the stage of phagophore formation. Atg30 recruits Atg37 to the pexophagic RPC, where Atg37 regulates the recruitment of the scaffold protein, Atg11. Palmitoyl-CoA competes with Atg30 for Atg37 binding. The human orthologue of Atg37, acyl-CoA–binding domain containing protein 5 (ACBD5), is also peroxisomal and is required specifically for pexophagy. We suggest that Atg37/ACBD5 is a new component and positive regulator of the pexophagic RPC.

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Authors
Nazarko, T. Y., Ozeki, K., Till, A., Ramakrishnan, G., Lotfi, P., Yan, M., & Subramani, S.
Affiliations
University of California San Diego (US)
Corresponding author
Subramani, Suresh
Venue
Journal of Cell Biology
Published
2014-02-17
Volume
204
Issue
4
Pages
541-557
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W1981927394
Cited by
99
References
57
Citations by year
2025: 6 · 2024: 4 · 2023: 6 · 2022: 3 · 2021: 5 · 2020: 12 · 2019: 14 · 2018: 15 · 2017: 8 · 2016: 12 · 2015: 10 · 2014: 4
FWCI
8.59
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • Deutsche Forschungsgemeinschaft
  • National Institutes of Health (GM085764, GM069373)
  • National Institute of General Medical Sciences (GM 085764, GM-069373, P50GM085764, R01GM069373)
  • National Institute of Diabetes and Digestive and Kidney Diseases (K01DK094843, DK094843)
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
pexophagy, Atg11, phagophore formation, peroxisome degradation, selective autophagy, autophagy receptors, palmitoyl-CoA, acyl-CoA binding protein, peroxisomal membrane proteins
MeSH terms
Huntingtin Protein, Sequestosome-1 Protein, Autophagy, Fungal Proteins, HeLa Cells, Humans, Image Processing, Computer-Assisted, Membrane Proteins, Microscopy, Fluorescence, Mutation, Nerve Tissue Proteins, Palmitoyl Coenzyme A, Phagosomes, Pichia, Peroxisomes, Immunoprecipitation, Adaptor Proteins, Signal Transducing

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