CHC22 and CHC17 clathrins have distinct biochemical properties and display differential regulation and function.

The Journal of Biological Chemistry
Philip N DannhauserF M Brodsky

Abstract

Clathrins are cytoplasmic proteins that play essential roles in endocytosis and other membrane traffic pathways. Upon recruitment to intracellular membranes, the canonical clathrin triskelion assembles into a polyhedral protein coat that facilitates vesicle formation and captures cargo molecules for transport. The triskelion is formed by trimerization of three clathrin heavy-chain subunits. Most vertebrates have two isoforms of clathrin heavy chains, CHC17 and CHC22, generating two clathrins with distinct cellular functions. CHC17 forms vesicles at the plasma membrane for receptor-mediated endocytosis and at the trans-Golgi network for organelle biogenesis. CHC22 plays a key role in intracellular targeting of the insulin-regulated glucose transporter 4 (GLUT4), accumulates at the site of GLUT4 sequestration during insulin resistance, and has also been implicated in neuronal development. Here, we demonstrate that CHC22 and CHC17 share morphological features, in that CHC22 forms a triskelion and latticed vesicle coats. However, cellular CHC22-coated vesicles were distinct from those formed by CHC17. The CHC22 coat was more stable to pH change and was not removed by the enzyme complex that disassembles the CHC17 coat. Moreover, th...Continue Reading

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Citations

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Methods Mentioned

BETA
electron microscopy
size-exclusion chromatography
fluorescence microscopy
fluorescence-activated cell sorter
transfection
FACS
co-immunoprecipitation
confocal microscopy
electrophoresis

Software Mentioned

NIH ImageJ
ImageJ
GraphPad Prism
DIVA

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