Structure, function, and regulation of myosin 1C

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 nec...

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Bibliographic Details
Published inActa biochimica Polonica Vol. 52; no. 2; pp. 373 - 380
Main Authors Barylko, Barbara, Jung, Gwanghyun, Albanesi, Joseph P
Format Journal Article
LanguageEnglish
Published Poland 01.01.2005
Subjects
Animals
Calmodulin - metabolism
Humans
Models, Biological
Myosin Type I - chemistry
Myosin Type I - metabolism
Myosin Type I - physiology
Protein Binding
Protein Conformation
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Summary: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.
ISSN:0001-527X
1734-154X
DOI:10.18388/abp.2005_3450