Interaction of a Golgi-Associated Kinesin-Like Protein with Rab6

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1998-01, Vol.279 (5350), p.580-585
Main Authors: Echard, Arnaud, Jollivet, Florence, Martinez, Olivier, Lacapère, Jean-Jacques, Rousselet, Annie, Janoueix-Lerosey, Isabelle, Goud, Bruno
Format: Article
Language:English
Subjects:
Adenosine triphosphatases
Adenosine Triphosphatases - metabolism
Alkaline Phosphatase - metabolism
Amino Acid Sequence
Amino acids
Antibodies
Biological and medical sciences
Biological Transport
Carrier Proteins - metabolism
Cell structures and functions
Complementary DNA
Endoplasmic Reticulum - metabolism
Fundamental and applied biological sciences. Psychology
Golgi apparatus
Golgi Apparatus - chemistry
Golgi Apparatus - metabolism
Golgi Apparatus - ultrastructure
GTPases
Guanosine triphosphatase
Guanosine Triphosphate - metabolism
HeLa Cells
Humans
Kinesin - analysis
Kinesin - chemistry
Kinesin - genetics
Kinesin - metabolism
Microtubules - metabolism
Microtubules - ultrastructure
Molecular and cellular biology
Molecular biology
Molecular Sequence Data
Molecular Weight
Physiological regulation
Plasmids
Proteins
rab GTP-Binding Proteins
ras Proteins - metabolism
Scientific Concepts
Vaccinia
Yeasts
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.279.5350.580