HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2 - PubMed (original) (raw)

. 2001 Oct 19;276(42):39271-6.

doi: 10.1074/jbc.C100401200. Epub 2001 Aug 21.

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• PMID: 11517213
• DOI: 10.1074/jbc.C100401200

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HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2

M Metzler et al. J Biol Chem. 2001.

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Abstract

Polyglutamine expansion in huntingtin is the underlying mutation leading to neurodegeneration in Huntington disease. This mutation influences the interaction of huntingtin with different proteins, including huntingtin-interacting protein 1 (HIP1), in which affinity to bind to mutant huntingtin is profoundly reduced. Here we demonstrate that HIP1 colocalizes with markers of clathrin-mediated endocytosis in neuronal cells and is highly enriched on clathrin-coated vesicles (CCVs) purified from brain homogenates. HIP1 binds to the clathrin adaptor protein 2 (AP2) and the terminal domain of the clathrin heavy chain, predominantly through a small fragment encompassing amino acids 276-335. This region, which contains consensus clathrin- and AP2-binding sites, functions in conjunction with the coiled-coil domain to target HIP1 to CCVs. Expression of various HIP1 fragments leads to a potent block of clathrin-mediated endocytosis. Our findings demonstrate that HIP1 is a novel component of the endocytic machinery.

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