Cargo regulates clathrin-coated pit invagination via clathrin light chain phosphorylation.

Autor: Maib H; Centre for Membrane Interactions and Dynamics, Department of Biomedical Science, University of Sheffield, Sheffield, UK., Ferreira F; Centre for Membrane Interactions and Dynamics, Department of Biomedical Science, University of Sheffield, Sheffield, UK., Vassilopoulos S; Sorbonne Université, INSERM, Institute of Myology, Centre for Research in Myology, UMRS 974, Paris, France., Smythe E; Centre for Membrane Interactions and Dynamics, Department of Biomedical Science, University of Sheffield, Sheffield, UK e.smythe@sheffield.ac.uk.
Jazyk: angličtina
Zdroj: The Journal of cell biology [J Cell Biol] 2018 Dec 03; Vol. 217 (12), pp. 4253-4266. Date of Electronic Publication: 2018 Sep 18.
DOI: 10.1083/jcb.201805005
Abstrakt: Clathrin light chains (CLCs) control selective uptake of a range of G protein-coupled receptors (GPCRs), although the mechanism by which this occurs has remained elusive thus far. In particular, site-specific phosphorylation of CLCb controls the uptake of the purinergic GPCR P2Y 12 , but it is dispensable for the constitutive uptake of the transferrin receptor (TfR). We demonstrate that phosphorylation of CLCb is required for the maturation of clathrin-coated pits (CCPs) through the transition of flat lattices into invaginated buds. This transition is dependent on efficient clathrin exchange regulated by CLCb phosphorylation and mediated through auxilin. Strikingly, this rearrangement is required for the uptake of P2Y 12 but not TfR. These findings link auxilin-mediated clathrin exchange to early stages of CCP invagination in a cargo-specific manner. This supports a model in which CCPs invaginate with variable modes of curvature depending on the cargo they incorporate.
(© 2018 Maib et al.)
Databáze: MEDLINE
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