Literature DB >> 17172850

Motors and their tethers: the role of secondary binding sites in processive motility.

Margaret M Kincaid1, Stephen J King.   

Abstract

Cytoskeletal motors convert the energy from binding and hydrolyzing ATP into conformational changes that direct movement along a cytoskeletal polymer substrate. These enzymes utilize different mechanisms to generate long-range motion on the order of a micron or more that is required for functions ranging from muscle contraction to transport of growth factors along a nerve axon. Several of the individual cytoskeletal motors are processive, meaning that they have the ability to take sequential steps along their polymer substrate without dissociating from the polymer. This ability to maintain contact with the polymer allows individual motors to move cargos quickly from one cellular location to another. Many of the processive motors have now been found to utilize secondary binding sites that aid in motor processivity.

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Year:  2006        PMID: 17172850      PMCID: PMC1850974          DOI: 10.4161/cc.5.23.3521

Source DB:  PubMed          Journal:  Cell Cycle        ISSN: 1551-4005            Impact factor:   4.534


  38 in total

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4.  Movement of microtubules by single kinesin molecules.

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7.  Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change.

Authors:  M Tomishige; R D Vale
Journal:  J Cell Biol       Date:  2000-11-27       Impact factor: 10.539

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Authors:  K S Thorn; J A Ubersax; R D Vale
Journal:  J Cell Biol       Date:  2000-11-27       Impact factor: 10.539

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Review 10.  Myosin V motor proteins: marching stepwise towards a mechanism.

Authors:  Ronald D Vale
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  10 in total

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5.  The trafficking protein GABARAP binds to and enhances plasma membrane expression and function of the angiotensin II type 1 receptor.

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8.  Cooperative protofilament switching emerges from inter-motor interference in multiple-motor transport.

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9.  Mitochondria-associated myosin 19 processively transports mitochondria on actin tracks in living cells.

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10.  Phospholipase C-related catalytically inactive protein (PRIP) controls KIF5B-mediated insulin secretion.

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  10 in total

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