Regulation of the enzymatic and motor activities of myosin I

Biochim Biophys Acta. 2000 Mar 17;1496(1):23-35. doi: 10.1016/s0167-4889(00)00006-9.

Abstract

Myosins I were the first unconventional myosins to be purified and they remain the best characterized. They have been implicated in various motile processes, including organelle translocation, ion channel gating and cytoskeletal reorganization but their exact cellular functions are still unclear. All members of the myosin I family, from yeast to man, have three structural domains: a catalytic head domain that binds ATP and actin; a tail domain believed to be involved in targeting the myosins to specific subcellular locations and a junction or neck domain that connects them and interacts with light chains. In this review we discuss how each of these three domains contributes to the regulation of myosin I enzymatic activity, motor activity and subcellular localization.

Publication types

  • Review

MeSH terms

  • Actins / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Catalytic Domain
  • Humans
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / genetics
  • Molecular Motor Proteins / metabolism*
  • Molecular Sequence Data
  • Myosins / chemistry*
  • Myosins / genetics
  • Myosins / metabolism*
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary

Substances

  • Actins
  • Molecular Motor Proteins
  • Adenosine Triphosphate
  • Myosins