[Mechanisms of action and cellular functions of molecular motors].
Cytoskeleton based molecular motors support most of the cellular movements and by consequence they are associated with a variety of human disorders. The wide functional diversity of these molecular motors is now explained by the presence of three different families: the myosin, kinesin and dynein families. Although they are functionally distinct, these motors present unexpected structural homologies at the ATP and actin or microtubule binding sites. However, these homologies do not seem sufficient to design a common molecular mechanism which allows these proteins to move along the cytoskeleton.
Centre de Recherches de Biochimie macromoléculaire, UPR1086 du CNRS, IFR24, Montpellier. patrick@xerxes.crbm.cnrs-mop.fr
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Chaussepied
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Smyczynski
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Van Dijk
D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003599:Cytoskeleton / Q000502:physiology*; D004194:Disease; D004398:Dyneins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000502:physiology; D008870:Microtubules / Q000502:physiology; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D009218:Myosins / Q000737:chemistry / Q000502:physiology; D011487:Protein Conformation
D000199:Actins; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D009218:Myosins; D004398:Dyneins; D016547:Kinesins
Mécanismes d'action et fonctions cellulaires des moteurs moléculaires.