HIP-I: a huntingtin interacting protein isolated by the yeast two- hybrid system |
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Authors: | Wanker EE; Rovira C; Scherzinger E; Hasenbank R; Walter S; Tait D; Colicelli J; Lehrach H |
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Institution: | Max Planck Institut fur Molekulare Genetik, Berlin (Dahlem), Germany. |
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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.
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