Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition.

Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C., Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B., Johansen T., Deretic V.

Autophagy, a homeostatic process whereby eukaryotic cells target cytoplasmic cargo for degradation, plays a broad role in health and disease states. Here we screened the TRIM family for roles in autophagy and found that half of TRIMs modulated autophagy. In mechanistic studies, we show that TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states. Furthermore, TRIM5α acts as a selective autophagy receptor. Based on direct sequence-specific recognition, TRIM5α delivered its cognate cytosolic target, a viral capsid protein, for autophagic degradation. Thus, our study establishes that TRIMs can function both as regulators of autophagy and as autophagic cargo receptors, and reveals a basis for selective autophagy in mammalian cells.

Dev. Cell 30:394-409(2014) [PubMed] [Europe PMC]

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again