Journal
JOURNAL OF CELL BIOLOGY
Volume 217, Issue 12, Pages 4253-4266Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201805005
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Funding
- Medical Research Council [MR/J001546/1]
- European Union [641639]
- Wellcome Trust [WT093134AIA]
- Medical Research Council SHI MA award [MR/K015753/1]
- MRC [MR/J001546/1, MR/K015753/1] Funding Source: UKRI
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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.
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