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HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system

Item Type:Article
Title:HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system
Creators Name:Wanker, E.E. and Rovira, C. and Scherzinger, E. and Hasenbank, R. and Walter, S. and Tait, D. and Colicelli, J. and Lehrach, H.
Abstract:We report the discovery of the huntingtin interacting protein I (HIP-I) which binds specifically to the N-terminus of human huntingtin, both in the two-hybrid screen and in in vitro binding experiments. For the interaction in vivo, a protein region downstream of the polyglutamine stretch in huntingtin is essential. The HIP1 cDNA isolated by the two-hybrid screen encodes a 55 kDa fragment of a novel protein. Using an affinity-purified polyclonal antibody raised against recombinant HIP-I, a protein of 116 kDa was detected in brain extracts by Western blot analysis. The predicted amino acid sequence of the HIP-I fragment exhibits significant similarity to cytoskeleton proteins, suggesting that HIP-I and huntingtin play a functional role in the cell filament networks. The HIP1 gene is ubiquitously expressed in different brain regions at low level. HIP-I is enriched in human brain but can also be detected in other human tissues as well as in mouse brain. HIP-I and huntingtin behave almost identically during subcellular fractionation and both proteins are enriched in the membrane containing fractions.
Keywords:Amino Acid Sequence, Northern Blotting, Western Blotting, Brain Chemistry, Molecular Cloning, Cytoskeleton, DNA-Binding Proteins, Polyacrylamide Gel Electrophoresis, Gene Expression, Huntington Disease, Molecular Sequence Data, Nerve Tissue Proteins, Nuclear Proteins, Peptides, Recombinant Fusion Proteins, Nucleic Acid Repetitive Sequences, Saccharomyces cerevisiae, Sequence Analysis
Source:Human Molecular Genetics
Publisher:Oxford University Press
Page Range:487-495
Date:1 March 1997
Official Publication:https://doi.org/10.1093/hmg/6.3.387
PubMed:View item in PubMed

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