Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin

• Published in: Molecular and cellular biochemistry Vol. 190; no. 1-2; pp. 133 - 141
• Main Authors: Kusano, K, Abe, H, Obinata, T
• Format: Journal Article
• Language: English
• Published: Netherlands Springer Nature B.V 01.01.1999
• Subjects: Actin Depolymerizing Factors; Actins - metabolism; Amino Acid Sequence; Animals; Bacteria; Bacteriology; Chickens; E coli; Microfilament Proteins - chemistry; Microfilament Proteins - genetics; Microfilament Proteins - metabolism; Molecular Sequence Data; Molecular weight; Peptides; Phosphatidylinositols - metabolism; Phosphorylation; Protein Binding; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Sequence Deletion; Sequence Homology, Amino Acid

Cofilin is an actin-binding protein of low molecular weight which is widely distributed in eukaryotes and is deeply involved in the dynamics of actin assembly in the cytoplasm. The actin-binding ability of cofilin is inhibited by inositol phosphates (PIP2), and the PIP2- and actin-binding site(s) ha...