Abstract
Most UNC-104/KIF1 kinesins are monomeric motors that transport membrane-bounded organelles toward the plus ends of microtubules. Recent evidence implies that KIF1A, a synaptic vesicle motor, moves processively. This surprising behavior for a monomeric motor depends upon a lysine-rich loop in KIF1A that binds to the negatively charged carboxyl terminus of tubulin and, in the context of motor processivity, compensates for the lack of a second motor domain on the KIF1A holoenzyme.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Biological Transport, Active
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Caenorhabditis elegans Proteins*
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Humans
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Kinesins / chemistry*
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Kinesins / metabolism
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Kinesins / physiology*
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Molecular Motor Proteins / chemistry
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Molecular Motor Proteins / metabolism
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Molecular Motor Proteins / physiology
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / metabolism
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Nerve Tissue Proteins / physiology*
Substances
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Caenorhabditis elegans Proteins
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KIF1A protein, human
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Molecular Motor Proteins
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Nerve Tissue Proteins
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UNC-104 protein, C elegans
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Kinesins