Huntingtin Interacting Protein 1 (HIP1)

ILWEQ

SPN	R323
HGNC	4913
MGI	1099804
PubMed	21947769
RGD	620305
UniProt	O00291
Wiki	HIP1

Huntingtin Interacting Protein is a protein that interacts with the huntingtin protein contain a domain homologous to the death effector domains (DED) found on proteins involved in apoptosis. It is believed that accumulation of high levels of the free form of this protein (free as in dissociated from the huntingtin and free to bind other key protein(s)) in the cell is one of the mechanisms by which neuron cell death is caused in Huntington's Disease (via the caspase-3 route). The role of Hip-1 in caspase mediated cell death remains unclear. Huntingtin interacting protein 1 (HIP1) was first identified by Wanker et al. in 1997. HIP1 was found to bind to Htt in an N-terminal dependent manner, and co-localise with Htt in the CNS although the nature of this interaction with respect to muHtt was not identified.

Reference

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"HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain."
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"HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin."
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"The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis."
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"HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2."
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"Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins."
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"HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain."
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"Huntingtin-interacting protein 1 is overexpressed in prostate and colon cancer and is critical for cellular survival."
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"HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains."
J. Biol. Chem. 279:14294-14306(2004) [PubMed] [Europe PMC] [Abstract]

"Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo."
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"Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors."
J. Cell Biol. 170:191-200(2005) [PubMed] [Europe PMC] [Abstract]

"Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-related protein) is regulated by clathrin light chain."
J. Biol. Chem. 283:32870-32879(2008) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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"Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding."
J. Mol. Biol. 367:8-15(2007) [PubMed] [Europe PMC] [Abstract]

"Crystal structure at 2.8 A of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI)."
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