Capping complex formation at the slow-growing end of the actin filament

Biochemistry (Mosc). 2008 Dec;73(13):1467-72. doi: 10.1134/s0006297908130075.

Abstract

Actin filaments are polar; their barbed (fast-growing) and pointed (slow-growing) ends differ in structure and dynamic properties. The slow-growing end is regulated by tropomodulins, a family of capping proteins that require tropomyosins for optimal function. There are four tropomodulin isoforms; their distributions vary depending on tissue type and change during development. The C-terminal half of tropomodulin contains one compact domain represented by alternating alpha-helices and beta-structures. The tropomyosin-independent actin-capping site is located at the C-terminus. The N-terminal half has no regular structure; however, it contains a tropomyosin-dependent actin-capping site and two tropomyosin-binding sites. One tropomodulin molecule can bind two tropomyosin molecules. Effectiveness of tropomodulin binding to tropomyosin depends on the tropomyosin isoform. Regulation of tropomodulin binding at the pointed end as well as capping effectiveness in the presence of specific tropomyosins may affect formation of local cytoskeleton and dynamics of actin filaments in cells.

Publication types

  • Review

MeSH terms

  • Actin Capping Proteins / chemistry
  • Actin Capping Proteins / metabolism*
  • Actin Cytoskeleton / chemistry*
  • Actin Cytoskeleton / metabolism*
  • Amino Acid Sequence
  • Binding Sites
  • Models, Molecular
  • Molecular Sequence Data
  • Muscle Proteins / chemistry
  • Muscle Proteins / metabolism
  • Substrate Specificity

Substances

  • Actin Capping Proteins
  • Muscle Proteins