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O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits

Clathrin-mediated endocytosis (CME) controls the internalization and function of a wide range of cell surface proteins. CME occurs by the assembly of clathrin and many other proteins on the inner leaflet of the plasma membrane into clathrin-coated pits (CCPs). These structures recruit specific cargo...

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Autores principales: Rahmani, Sadia, Ahmed, Hafsa, Ibazebo, Osemudiamen, Fussner-Dupas, Eden, Wakarchuk, Warren W., Antonescu, Costin N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9999237/
https://www.ncbi.nlm.nih.gov/pubmed/36731797
http://dx.doi.org/10.1016/j.jbc.2023.102963
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author Rahmani, Sadia
Ahmed, Hafsa
Ibazebo, Osemudiamen
Fussner-Dupas, Eden
Wakarchuk, Warren W.
Antonescu, Costin N.
author_facet Rahmani, Sadia
Ahmed, Hafsa
Ibazebo, Osemudiamen
Fussner-Dupas, Eden
Wakarchuk, Warren W.
Antonescu, Costin N.
author_sort Rahmani, Sadia
collection PubMed
description Clathrin-mediated endocytosis (CME) controls the internalization and function of a wide range of cell surface proteins. CME occurs by the assembly of clathrin and many other proteins on the inner leaflet of the plasma membrane into clathrin-coated pits (CCPs). These structures recruit specific cargo destined for internalization, generate membrane curvature, and in many cases undergo scission from the plasma membrane to yield intracellular vesicles. The diversity of functions of cell surface proteins controlled via internalization by CME may suggest that regulation of CCP formation could be effective to allow cellular adaptation under different contexts. Of interest is how cues derived from cellular metabolism may regulate CME, given the reciprocal role of CME in controlling cellular metabolism. The modification of proteins with O-linked β-GlcNAc (O-GlcNAc) is sensitive to nutrient availability and may allow cellular adaptation to different metabolic conditions. Here, we examined how the modification of proteins with O-GlcNAc may control CCP formation and thus CME. We used perturbation of key enzymes responsible for protein O-GlcNAc modification, as well as specific mutants of the endocytic regulator AAK1 predicted to be impaired for O-GlcNAc modification. We identify that CCP initiation and the assembly of clathrin and other proteins within CCPs are controlled by O-GlcNAc protein modification. This reveals a new dimension of regulation of CME and highlights the important reciprocal regulation of cellular metabolism and endocytosis.
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spelling pubmed-99992372023-03-11 O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits Rahmani, Sadia Ahmed, Hafsa Ibazebo, Osemudiamen Fussner-Dupas, Eden Wakarchuk, Warren W. Antonescu, Costin N. J Biol Chem Research Article Clathrin-mediated endocytosis (CME) controls the internalization and function of a wide range of cell surface proteins. CME occurs by the assembly of clathrin and many other proteins on the inner leaflet of the plasma membrane into clathrin-coated pits (CCPs). These structures recruit specific cargo destined for internalization, generate membrane curvature, and in many cases undergo scission from the plasma membrane to yield intracellular vesicles. The diversity of functions of cell surface proteins controlled via internalization by CME may suggest that regulation of CCP formation could be effective to allow cellular adaptation under different contexts. Of interest is how cues derived from cellular metabolism may regulate CME, given the reciprocal role of CME in controlling cellular metabolism. The modification of proteins with O-linked β-GlcNAc (O-GlcNAc) is sensitive to nutrient availability and may allow cellular adaptation to different metabolic conditions. Here, we examined how the modification of proteins with O-GlcNAc may control CCP formation and thus CME. We used perturbation of key enzymes responsible for protein O-GlcNAc modification, as well as specific mutants of the endocytic regulator AAK1 predicted to be impaired for O-GlcNAc modification. We identify that CCP initiation and the assembly of clathrin and other proteins within CCPs are controlled by O-GlcNAc protein modification. This reveals a new dimension of regulation of CME and highlights the important reciprocal regulation of cellular metabolism and endocytosis. American Society for Biochemistry and Molecular Biology 2023-01-31 /pmc/articles/PMC9999237/ /pubmed/36731797 http://dx.doi.org/10.1016/j.jbc.2023.102963 Text en © 2023 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Rahmani, Sadia
Ahmed, Hafsa
Ibazebo, Osemudiamen
Fussner-Dupas, Eden
Wakarchuk, Warren W.
Antonescu, Costin N.
O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
title O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
title_full O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
title_fullStr O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
title_full_unstemmed O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
title_short O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
title_sort o-glcnac transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9999237/
https://www.ncbi.nlm.nih.gov/pubmed/36731797
http://dx.doi.org/10.1016/j.jbc.2023.102963
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