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Molecular cloning of a novel actin‐binding protein, p57, with a WD repeat and a leucine zipper motif
Author(s) -
Suzuki Kensuke,
Nishihata Jun,
Arai Yuko,
Honma Nakayuki,
Yamamoto Kazuo,
Irimura Tatsuro,
Toyoshima Satoshi
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00393-n
Subject(s) - leucine zipper , biology , dictyostelium discoideum , cytokinesis , peptide sequence , microbiology and biotechnology , pleckstrin homology domain , sequence motif , complementary dna , bzip domain , biochemistry , cell division , signal transduction , cell , dna , gene
A 57 kDa protein (p57) was obtained during the study on phosphatidylinositol‐specific phospholipase C. Its cDNA was isolated from calf spleen and human leukemia cell line HL60 libraries and cloned. In the primary structures of p57, they have two unique amino acid sequence motifs, a WD repeat and a leucine zipper motif. Furthermore, p57 shared sequence similarity (40%) with coronin, an actin‐binding protein responsible for chemotaxis, cell motility, and cytokinesis of Dictyostelium discoideum , which has only the WD repeat. p57 also showed an actin‐binding activity and was mainly expressed in immune tissues. From these results, we conclude that p57 is a coronin‐like novel actin‐binding protein in mammalian cells but may also have a different function from coronin.