Localization and identification of actin structures involved in the filamin-actin interaction

Eur J Biochem. 1992 Oct 15;209(2):555-62. doi: 10.1111/j.1432-1033.1992.tb17320.x.

Abstract

The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105-120 and 360-372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry*
  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / metabolism
  • Chickens
  • Contractile Proteins / isolation & purification
  • Contractile Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Filamins
  • Fluorescent Dyes
  • Kinetics
  • Microfilament Proteins / isolation & purification
  • Microfilament Proteins / metabolism*
  • Muscle, Smooth / metabolism
  • Muscles / metabolism
  • Naphthalenesulfonates
  • Peptide Fragments / isolation & purification
  • Protein Binding
  • Rabbits
  • Tropomyosin / metabolism

Substances

  • Actins
  • Carrier Proteins
  • Contractile Proteins
  • Filamins
  • Fluorescent Dyes
  • Microfilament Proteins
  • Naphthalenesulfonates
  • Peptide Fragments
  • Tropomyosin
  • 1,5-I-AEDANS