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RAB33B recruits the...
RAB33B recruits the ATG16L1 complex to the phagophore via a noncanonical RAB binding protein
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- Pantoom, Supansa (author)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR),Translational Neurodegeneration Section "Albrecht-kossel", Department of Neurology, University Medical Center Rostock, Rostock, Germany
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- Konstantinidis, Georgios (author)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR),Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Crete, Greece
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Voss, Stephanie (author)
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Han, Hongmei (author)
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Hofnagel, Oliver (author)
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Li, Zhiyu (author)
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- Wu, Yao-Wen, Professor (author)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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(creator_code:org_t)
- 2020-09-22
- 2021
- English.
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In: Autophagy. - : Taylor & Francis. - 1554-8627 .- 1554-8635. ; 17:9, s. 2290-2304
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Abstract
Subject headings
Close
- Autophagosome formation is a fundamental process in macroautophagy/autophagy, a conserved self-eating mechanism in all eukaryotes, which requires the conjugating ATG (autophagy related) protein complex, ATG12-ATG5-ATG16L1 and lipidated MAP1LC3/LC3 (microtubule associated protein 1 light chain 3). How the ATG12-ATG5-ATG16L1 complex is recruited to membranes is not fully understood. Here, we demonstrated that RAB33B plays a key role in recruiting the ATG16L1 complex to phagophores during starvation-induced autophagy. Crystal structures of RAB33B bound to the coiled-coil domain (CCD) of ATG16L1 revealed the recognition mechanism between RAB33B and ATG16L1. ATG16L1 is a novel RAB-binding protein (RBP) that can induce RAB proteins to adopt active conformation without nucleotide exchange. RAB33B and ATG16L1 mutually determined the localization of each other on phagophores. RAB33B-ATG16L1 interaction was required for LC3 lipidation and autophagosome formation. Upon starvation, a fraction of RAB33B translocated from the Golgi to phagophores and recruited the ATG16L1 complex. In this work, we reported a new mechanism for the recruitment of the ATG12-ATG5-ATG16L1 complex to phagophores by RAB33B, which is required for autophagosome formation.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Keyword
- autophagosome formation
- autophagy
- crystal structure
- RAB33B
Publication and Content Type
- ref (subject category)
- art (subject category)
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