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Exp Cell Res. 1999 Dec 15;253(2):673-80.

Domain analysis of the actin-binding and actin-remodeling activities of drebrin.

Author information

1
Department of Neurobiology and Behavior, Department of Pharmacology, Gunma University School of Medicine, 3-39-22 Showamachi, Maebashi, 371, Japan. hayashi@sb.gunma-u.ac.jp

Abstract

Drebrin is an actin-binding protein which is expressed at highly levels in neurons. When introduced into fibroblasts, it has been known to bind to F-actin and to cause remodeling of F-actin. Here, we performed a domain analysis of the actin-binding and actin-remodeling activities of drebrin. Various fragments of drebrin cDNA were fused with green fluorescent protein cDNA and introduced into Chinese hamster ovary cells. Association of the fusion protein with F-actin and remodeling of the F-actin were examined. We found that the central 85-amino-acid sequence (residues 233-317) was sufficient for the binding to and remodeling of F-actin. The binding activity of this fragment was relatively low compared with that of full-length drebrin, but all the types of abnormalities of F-actin that are observed with full-length drebrin were also observed with this fragment. When this sequence was further fragmented, the actin-binding activity was greatly reduced and the actin-remodeling activity disappeared. The actin-binding activity of the central region of drebrin was confirmed by a cosedimentation assay of chymotryptic fragments of drebrin with purified actin. These data indicate that the actin-binding domain and actin-remodeling domain are identical and that this domain is located at the central region of drebrin.

PMID:
10585290
DOI:
10.1006/excr.1999.4663
[Indexed for MEDLINE]

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