hDKIR, a human homologue of the Drosophila kelch protein, involved in a ring-like structure.

We have previously purified and cloned an apoptosis-inducing protein (AIP) derived from fish infected with the anisakis simplex. Recently, we identified a series of AIP-responsive genes in the HL-60 cell line using a subtractive hybridization method. Here we report the molecular cloning and characterization of one of these genes, which ...
encodes a novel human kelch protein containing 568 amino acid residues, termed hDKIR. The Drosophila Kelch protein localizes to a ring canal structure, which is required for oocyte development. When hDKIR was expressed in cultured-mammalian cells, hDKIR localized to a ring-like structure. Furthermore, when coexpressed with Mayven or Keap1, hDKIR bound to Mayven and recruited Mayven into ring-like structures perfectly. This indicates that kelch homologues can interact with each other in a specific manner and such interaction can affect the subcellular localization of kelch proteins. Finally, domain analysis revealed that both the N-terminal POZ (poxviruses and zinc fingers) and intervening region (IVR) domains of hDKIR are essential for ring-like structure activity, suggesting that the development of the ring-like structure is independent of the ability to bind actin.
Mesh Terms:
Actin Cytoskeleton, Actins, Animals, Binding Sites, CHO Cells, Carrier Proteins, Cloning, Molecular, Cricetinae, DNA, Complementary, Drosophila Proteins, Fluorescent Antibody Technique, HeLa Cells, Humans, Microfilament Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Organelles, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid
Exp. Cell Res.
Date: Oct. 15, 2004
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