Anti-HIP1R Antibody Picoband® Fluoro647 Conjugated

Huntingtin-interacting protein 1-related protein is a protein that in humans is encoded by the HIP1R gene. Huntingtin-interacting protein 1-related protein, or HIP1R, was identified on the basis of its structural homology with Huntingtin-interacting protein 1, or HIP1. Based on its domain structure, HIP1R is a putative endocytosis-related protein. Knockdown of HIP1R impairs the endocytosis of activated epidermal growth factor receptor (EGFR) and the consequent activation of the downstream ERK and Akt proteins. Additionally, HIP1R is a component of the clathrin-coated pits and vesicles, which in part links the endocytic machinery to the actin cytoskeleton. It binds to 3-phosphoinositides via ENTH domains to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. HIP1R deficiency significantly reduces the expression of the ionotropic glutamate receptor GluA1, GluN2A, and GluN2B subunits, but not the GABAA receptor α1 subunit. Knockdown of HIP1R reduces the amplitude and frequency of the miniature excitatory postsynaptic current, but not of the miniature inhibitory postsynaptic curren. HIP1R has been identified as a protein that can target histone deacetylase-3-mediated neurodegeneration, along with other proteins like NPTX1, NFL, TEX10, and TGFFG.

Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation (PubMed:17719545 PubMed:17681131, PubMed:23486064) . Also involved in promoting ciliogenesis. May play a role in the assembly of the mother centriole subdistal appendages (SDA) thereby effecting the fusion of recycling endosomes to basal bodies during cilia formation (By similarity) . Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2 (PubMed:16760425) .

1. Bradley, S. V., Hyun, T. S., Oravecz-Wilson, K. I., Li, L., Waldorff, E. I., Ermilov, A. N., Goldstein, S. A., Zhang, C. X., Drubin, D. G., Varela, K., Parlow, A., Dlugosz, A. A., Ross, T. S. Degenerative phenotypes caused by the combined deficiency of murine HIP1 and HIP1r are rescued by human HIP1. Hum. Molec. Genet. 16: 1279-1292, 2007. 2. Chopra, V. S., Metzler, M., Rasper, D. M., Engqvist-Goldstein, A. E. Y., Singaraja, R., Gan, L., Fichter, K. M., McCutcheon, K., Drubin, D., Nicholson, D. W., Hayden, M. R. HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin. Mammalian Genome 11: 1006-1015, 2000. 3. Engqvist-Goldstein, A. E. Y., Kessels, M. M., Chopra, V. S., Hayden, M. R., Drubin, D. G. An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J. Cell Biol. 147: 1503-1518, 1999.