Abstract
To further elucidate the mechanism of organelle transport, we cloned a novel member of the mouse kinesin superfamily, KIF1B. This N-terminal-type motor protein is expressed ubiquitously in various kinds of tissues. In situ hybridization revealed that KIF1B is expressed abundantly in differentiated nerve cells. Interestingly, K1F1B works as a monomer, having a microtubule plus end-directed motility. Our rotary shadowing electron microscopy revealed mostly single globular structures. Immunocytochemically, KIF1B was colocalized with mitochondria in vivo. Furthermore, a subcellular fractionation study showed that KIF1B was concentrated in the mitochondrial fraction, and purified K1F1B could transport mitochondria along microtubules in vitro. These data strongly suggested that KIF1B works as a monomeric motor for anterograde transport of mitochondria.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Axonal Transport / physiology*
-
Biological Transport / physiology
-
Cells, Cultured
-
Cloning, Molecular
-
Gene Expression Regulation, Developmental
-
Kinesins / chemistry
-
Kinesins / genetics
-
Kinesins / physiology*
-
Mice
-
Microtubule-Associated Proteins / chemistry
-
Microtubule-Associated Proteins / genetics
-
Microtubule-Associated Proteins / physiology*
-
Mitochondria / physiology*
-
Molecular Sequence Data
-
Movement / physiology
-
Nerve Tissue Proteins / chemistry
-
Nerve Tissue Proteins / genetics
-
Nerve Tissue Proteins / physiology*
-
Protein Structure, Secondary
-
Rats
-
Recombinant Proteins / chemistry
-
Sequence Homology, Amino Acid
-
Tissue Distribution
Substances
-
Kif1b protein, mouse
-
Kif1b protein, rat
-
Microtubule-Associated Proteins
-
Nerve Tissue Proteins
-
Recombinant Proteins
-
Kinesins