Membrane remodeling via ubiquitin-mediated pathways.

Cell Chem Biol

Goethe University Frankfurt, Medical Faculty, Institute of Biochemistry II, Theodor-Stern-Kai 7, 60590 Frankfurt Am Main, Germany; Goethe University Frankfurt, Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Strasse 15, 60438 Frankfurt Am Main, Germany. Electronic address:

Published: September 2024

The dynamic process of membrane shaping and remodeling plays a vital role in cellular functions, with proteins and cellular membranes interacting intricately to adapt to various cellular needs and environmental cues. Ubiquitination-a posttranslational modification-was shown to be essential in regulating membrane structure and shape. It influences virtually all pathways relying on cellular membranes, such as endocytosis and autophagy by directing protein degradation, sorting, and oligomerization. Ubiquitin is mostly known as a protein modifier; however, it was reported that ubiquitin and ubiquitin-like proteins can associate directly with lipids, affecting membrane curvature and dynamics. In this review, we summarize some of the current knowledge on ubiquitin-mediated membrane remodeling in the context of endocytosis, autophagy, and ER-phagy.

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http://dx.doi.org/10.1016/j.chembiol.2024.08.007DOI Listing

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