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PMID: 6890875 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF).

Cell motility ·Vol. 2 ·No. 1 ·1982-00-00 ·Pages 1-8

Bernstein BW, Bamburg JR

Abstract

Brain or muscle F-actin is rapidly depolymerized to monomeric actin in vitro by actin-depolymerizing factor, a protein isolated from chick embryo brain. Binding of muscle tropomyosin to muscle F-actin protects the F-actin from depolymerization by this factor. A 8.4/1.0 molar ratio of actin subunits to tropomyosin, achieved by incubation of the F-actin with excess tropomyosin, protects 58% of the F-actin from depolymerization by excess actin-depolymerizing factor for at least 3 hr at 25 degrees C. Thus, actin-depolymerizing factor seems to be specifically directed toward actin filaments lacking tropomyosin.

MeSH Terms
Actin Depolymerizing Factors Actins/metabolism Animals Brain/metabolism Chick Embryo Cytoskeleton/drug effects,metabolism Destrin In Vitro Techniques Microfilament Proteins Muscles/metabolism Protein Conformation/drug effects Proteins/pharmacology Rabbits Tropomyosin/metabolism
Chemicals
Actin Depolymerizing Factors Actins Destrin Microfilament Proteins Proteins Tropomyosin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bernstein B W
Bamburg J R
Article Info
Journal
Cell motility
Abbr.
Cell Motil
ISSN
0271-6585
Published
1982-00-00
Pages
1-8
Language
English
Region
United States
NLM ID
8207421
Subset
IM
Grants
NINDS NIH HHS · NS 10429 · United States
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