The actin-depolymerizing factor destrin has an actin-stabilizing domain

Authors
Tokuraku, K Okamoto, S Katsuki, M Nakagawa, H Kotani, S
Citation
K. Tokuraku et al., The actin-depolymerizing factor destrin has an actin-stabilizing domain, BIOC CELL B, 79(6), 2001, pp. 773-778
Citations number
24
Categorie Soggetti
Cell & Developmental Biology
Journal title
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE
ISSN journal
08298211 → ACNP
Volume
79
Issue
6
Year of publication
2001
Pages
773 - 778
Database
ISI
SICI code
0829-8211(200112)79:6<773:TAFDHA>2.0.ZU;2-2
Abstract
Destrin is a 19 kDa actin-depolymerizing protein of the ADF-cofilin family. Destrin was digested with trypsin to a structurally stable 9.2 kDa fragmen t that contains the actin-binding sequence. The purified 9.2 kDa fragment h as an actin filament stabilizing activity, rather than an actin filament de polymerizing activity. The deleted region is probably essential for the act in filament depolymerizing activity of intact destrin. Surprisingly, the 9. 2 kDa fragment also has an assembly-promoting activity in the absence of AT P.