Journal Article

The huntingtin interacting protein HIP1 is a clathrin and α-adaptin-binding protein involved in receptor-mediated endocytosis

Stephanie Waelter, Eberhard Scherzinger, Renate Hasenbank, Eckhard Nordhoff, Rudi Lurz, Heike Goehler, Christine Gauss, Kirupa Sathasivam, Gillian P. Bates, Hans Lehrach and Erich E. Wanker

in Human Molecular Genetics

Volume 10, issue 17, pages 1807-1817
Published in print August 2001 | ISSN: 0964-6906
Published online August 2001 | e-ISSN: 1460-2083 | DOI: http://dx.doi.org/10.1093/hmg/10.17.1807
The huntingtin interacting protein HIP1 is a clathrin and α-adaptin-binding protein involved in receptor-mediated endocytosis

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The huntingtin interacting protein (HIP1) is enriched in membrane-containing cell fractions and has been implicated in vesicle trafficking. It is a multidomain protein containing an N-terminal ENTH domain, a central coiled-coil forming region and a C-terminal actin-binding domain. In the present study we have identified three HIP1 associated proteins, clathrin heavy chain and α-adaptin A and C. In vitro binding studies revealed that the central coiled-coil domain is required for the interaction of HIP1 with clathrin, whereas DPF-like motifs located upstream to this domain are important for the binding of HIP1 to the C-terminal ‘appendage’ domain of α-adaptin A and C. Expression of full length HIP1 in mammalian cells resulted in a punctate cytoplasmic immunostaining characteristic of clathrin-coated vesicles. In contrast, when a truncated HIP1 protein containing both the DPF-like motifs and the coiled-coil domain was overexpressed, large perinuclear vesicle-like structures containing HIP1, huntingtin, clathrin and endocytosed transferrin were observed, indicating that HIP1 is an endocytic protein, the structural integrity of which is crucial for maintenance of normal vesicle size in vivo.

Journal Article.  7236 words.  Illustrated.

Subjects: Genetics and Genomics

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