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2005 | 52 | 2 | 373-380
Article title

Structure, function, and regulation of myosin 1C.

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EN
Abstracts
EN
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.
Publisher

Year
Volume
52
Issue
2
Pages
373-380
Physical description
Dates
published
2005
received
2005-04-25
revised
2005-05-05
accepted
2005-05-06
(unknown)
2005-05-31
Contributors
  • Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA;
  • Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA;
  • Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA;
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Document Type
Publication order reference
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YADDA identifier
bwmeta1.element.bwnjournal-article-abpv52i2p373kz
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