BERP, a novel ring finger protein, binds to alpha-actinin-4.
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.
Mesh Terms:
Actinin, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Brain, Cell Line, Chickens, Humans, Mice, Molecular Sequence Data, Nerve Tissue Proteins, PC12 Cells, Protein Isoforms, Rats, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transfection, Zinc Fingers
Actinin, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Brain, Cell Line, Chickens, Humans, Mice, Molecular Sequence Data, Nerve Tissue Proteins, PC12 Cells, Protein Isoforms, Rats, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transfection, Zinc Fingers
Biochem. Biophys. Res. Commun.
Date: Jan. 27, 2000
PubMed ID: 10673389
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