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Biochem Biophys Res Commun. 2000 Jan 27;267(3):906-11.

BERP, a novel ring finger protein, binds to alpha-actinin-4.

Author information

1
Graduate Program in Neuroscience, Department of Psychiatry, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.

Abstract

We recently identified BERP as a novel RING finger protein belonging to the RBCC protein family. It contains an N-terminal RING finger, followed by a B-box zinc finger and a coiled-coil domain. BERP interacts with the tail domain of the class V myosins through a beta-propeller structure in the BERP C-terminal. To identify other proteins interacting with BERP, the yeast two-hybrid strategy was employed, using the RBCC domain as bait. Screening of a rat brain cDNA library identified alpha-actinin-4 as a specific binding partner for the N-terminus of BERP. This actinin isoform could be immunoprecipitated together with BERP from HEK 293 cells transfected with expression constructs for BERP and alpha-actinin-4. These proteins could also be colocalized immunohistochemically in the cytoplasm of differentiated PC12 cells. We suggest that BERP may anchor class V myosins to particular cell domains via its interaction with alpha-actinin-4.

PMID:
10673389
DOI:
10.1006/bbrc.1999.2045
[Indexed for MEDLINE]

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