Augmentation of alpha-actinin-induced gelation of actin by talin

Interactions among the three major constituents of focal adhesions, talin, actin, and alpha-actinin, were studied. No evidence was obtained for the direct interaction between talin and alpha-actinin. Both talin and alpha-actinin increased the rate and extent of polymerization of actin, and their eff...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-03, Vol.267 (8), p.5621-5624
Main Authors: Muguruma, M. (Kyushu University, Fukuoka, Japan), Matsumura, S, Fukazawa, T
Format: Article
Language:English
Subjects:
actin
Actinin - chemistry
Actinin - isolation & purification
Actinin - metabolism
Actins - chemistry
Actins - isolation & purification
Actins - metabolism
alpha -actinin
Analytical, structural and metabolic biochemistry
Animals
AVES DE CORRAL
Biological and medical sciences
Chickens
Contractile proteins
Cross-Linking Reagents - pharmacology
Dimethyl Suberimidate - pharmacology
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
gelation
GELIFICACION
GELIFICATION
Gels
GESIER
Gizzard, Avian
GLOBULINAS
GLOBULINE
Holoproteins
induction
Kinetics
Macromolecular Substances
Molecular Weight
MOLLEJA (ESTOMAGO)
MUSCLE
Muscle, Smooth - metabolism
Muscles - metabolism
MUSCULOS
POLIMERIZACION
POLYMERISATION
polymerization
Protein Binding
Proteins
Rabbits
talin
Talin - chemistry
Talin - isolation & purification
Talin - metabolism
VOLAILLE
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Summary:Interactions among the three major constituents of focal adhesions, talin, actin, and alpha-actinin, were studied. No evidence was obtained for the direct interaction between talin and alpha-actinin. Both talin and alpha-actinin increased the rate and extent of polymerization of actin, and their effects were additive. Whereas talin alone exhibited very little actin-gelating activity, it potentiated markedly the gelation in the presence of alpha-actinin and lowered the concentration of alpha-actinin necessary for the gel formation. Its gelation-potentiating activity on prepolymerized actin was much smaller than observed on G-actin. Treatment of talin with a cross-linking reagent, 1-ethyl-3[3-(dimethylamino)-propyl]carbodiimide or dimethyl suberimidate, resulted in the formation of its oligomeric polypeptides. The complexes of talin and G-actin were also demonstrated with the cross-linking reagents and fluorescence-labeled actin. These results indicate that talin is able to cross-link some limited regions of actin filaments
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)42810-4