Abstract
Rab guanosine triphosphatases regulate vesicular transport and membrane traffic within eukaryotic cells. Here, a kinesin-like protein that interacts with guanosine triphosphate (GTP)-bound forms of Rab6 was identified. This protein, termed Rabkinesin-6, was localized to the Golgi apparatus and shown to play a role in the dynamics of this organelle. The carboxyl-terminal domain of Rabkinesin-6, which contains the Rab6-interacting domain, inhibited the effects of Rab6-GTP on intracellular transport. Thus, a molecular motor is a potential effector of a Rab protein, and coordinated action between members of these two families of proteins could control membrane dynamics and directional vesicular traffic.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / metabolism
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Alkaline Phosphatase / metabolism
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Amino Acid Sequence
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Biological Transport
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Carrier Proteins / metabolism*
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Endoplasmic Reticulum / metabolism
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Golgi Apparatus / chemistry
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Golgi Apparatus / metabolism*
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Golgi Apparatus / ultrastructure
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Guanosine Triphosphate / metabolism
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HeLa Cells
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Humans
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Kinesins / analysis
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Kinesins / chemistry
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Kinesins / genetics
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Kinesins / metabolism*
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Microtubules / metabolism
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Microtubules / ultrastructure
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Molecular Sequence Data
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Molecular Weight
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rab GTP-Binding Proteins*
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ras Proteins / metabolism*
Substances
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Carrier Proteins
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KIF20A protein, human
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Rab6 protein
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Guanosine Triphosphate
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Alkaline Phosphatase
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Adenosine Triphosphatases
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Kinesins
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rab GTP-Binding Proteins
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ras Proteins