Structure and evolution of the actin crosslinking proteins

Bioessays. 1991 May;13(5):219-26. doi: 10.1002/bies.950130504.

Abstract

The actin crosslinking proteins exhibit marked diversity in size and shape and crosslink actin filaments in different ways. Amino acid sequence analysis of many of these proteins has provided clues to the origin of their diversity. Spectrin, alpha-actinin, ABP-120, ABP-280, fimbrin, and dystrophin share a homologous sequence segment that is implicated as the common actin binding domain. The remainder of each protein consists of repetitive and non-repetitive sequence segments that have been shuffled and multiplied in evolution to produce a variety of proteins that are related in function and in composition, but that differ significantly in structure.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Actinin / genetics
  • Actinin / metabolism
  • Actinin / ultrastructure
  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Biological Evolution
  • Carrier Proteins / metabolism
  • Carrier Proteins / ultrastructure
  • Consensus Sequence
  • Dystrophin / genetics
  • Dystrophin / ultrastructure
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Microfilament Proteins / ultrastructure*
  • Molecular Sequence Data
  • Multigene Family
  • Spectrin / genetics
  • Spectrin / metabolism
  • Spectrin / ultrastructure
  • Structure-Activity Relationship

Substances

  • Actins
  • Carrier Proteins
  • Dystrophin
  • Membrane Glycoproteins
  • Microfilament Proteins
  • plastin
  • Actinin
  • Spectrin
  • abpC protein, Dictyostelium