TY - JOUR
T1 - Structure, function, and regulation of myosin 1C
AU - Barylko, Barbara
AU - Jung, Gwanghyun
AU - Albanesi, Joseph P.
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
KW - Domain structure
KW - Membrane protein translocation
KW - Myosin 1
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U2 - 10.18388/abp.2005_3450
DO - 10.18388/abp.2005_3450
M3 - Review article
C2 - 15933767
AN - SCOPUS:23644434254
SN - 0001-527X
VL - 52
SP - 373
EP - 380
JO - Acta Biochimica Polonica
JF - Acta Biochimica Polonica
IS - 2
ER -