Structure, function, and regulation of myosin 1C

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Myosin 1C, the first mammalian single-headed myosin to be purified, cloned, and sequenced, has been implicated in the translocation of plasma membrane channels and transporters. Like other forms of myosin I (of which eight exist in humans) myosin 1C consists of motor, neck, and tail domains. The neck domain binds calmodulins more tightly in the absence than in the presence of Ca 2+. Release of calmodulins exposes binding sites for anionic lipids, particularly phosphoinositides. The tail domain, which has an isoelectic point of 10.5, interacts with anionic lipid headgroups. When both neck and tail lipid binding sites are engaged, the myosin associates essentially irreversibly with membranes. Despite this tight membrane binding, it is widely believed that myosin 1C docking proteins are necessary for targeting the enzyme to specific subcellular location. The search for these putative myosin 1C receptors is an active area of research.

Original languageEnglish (US)
Pages (from-to)373-380
Number of pages8
JournalActa Biochimica Polonica
Volume52
Issue number2
StatePublished - 2005

Fingerprint

Myosins
Tail
Neck
Calmodulin
Lipids
Myosin Type I
Binding Sites
Membranes
Membrane Transport Proteins
Protein Transport
Cell membranes
Phosphatidylinositols
Ion Channels
Cell Membrane
Enzymes
Research
Proteins

Keywords

  • Domain structure
  • Membrane protein translocation
  • Myosin 1

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Structure, function, and regulation of myosin 1C. / Barylko, Barbara; Jung, Gwanghyun; Albanesi, Joseph P.

In: Acta Biochimica Polonica, Vol. 52, No. 2, 2005, p. 373-380.

Research output: Contribution to journalArticle

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