TY - JOUR
T1 - KIF3C and KIF3A form a novel neuronal heteromeric kinesin that associates with membrane vesicles
AU - Muresan, Virgil
AU - Abramson, Tatiana
AU - Lyass, Asya
AU - Winter, Dirk
AU - Porro, Elena
AU - Hong, Filbert
AU - Chamberlin, Nancy L.
AU - Schnapp, Bruce J.
PY - 1998
Y1 - 1998
N2 - We have cloned from rat brain the cDNA encoding an 89,828-Da kinesin- related polypeptide KIF3C that is enriched in brain, retina, and lung. Immunocytochemistry of hippocampal neurons in culture shows that KIF3C is localized to cell bodies, dendrites, and, in lesser amounts, to axons. In subcellular fractionation experiments, KIF3C cofractionates with a distinct population of membrane vesicles. Native KIF3C binds to microtubules in a kinesin-like, nucleotide-dependent manner. KIF3C is most similar to mouse KIF3B and KIF3A, two closely related kinesins that are normally present as a heteromer. In sucrose density gradients, KIF3C sediments at two distinct densities, suggesting that it may be part of two different multimolecular complexes. Immunoprecipitation experiments show that KIF3C is in part associated with KIF3A, but not with KIF3B. Unlike KIF3B, a significant portion of KIF3C is not associated with KIF3A. Consistent with these biochemical properties, the distribution of KIF3C in the CNS has both similarities and differences compared with KIF3A and KIF3B. These results suggest that KIF3C is a vesicle-associated motor that functions both independently and in association with KIF3A.
AB - We have cloned from rat brain the cDNA encoding an 89,828-Da kinesin- related polypeptide KIF3C that is enriched in brain, retina, and lung. Immunocytochemistry of hippocampal neurons in culture shows that KIF3C is localized to cell bodies, dendrites, and, in lesser amounts, to axons. In subcellular fractionation experiments, KIF3C cofractionates with a distinct population of membrane vesicles. Native KIF3C binds to microtubules in a kinesin-like, nucleotide-dependent manner. KIF3C is most similar to mouse KIF3B and KIF3A, two closely related kinesins that are normally present as a heteromer. In sucrose density gradients, KIF3C sediments at two distinct densities, suggesting that it may be part of two different multimolecular complexes. Immunoprecipitation experiments show that KIF3C is in part associated with KIF3A, but not with KIF3B. Unlike KIF3B, a significant portion of KIF3C is not associated with KIF3A. Consistent with these biochemical properties, the distribution of KIF3C in the CNS has both similarities and differences compared with KIF3A and KIF3B. These results suggest that KIF3C is a vesicle-associated motor that functions both independently and in association with KIF3A.
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U2 - 10.1091/mbc.9.3.637
DO - 10.1091/mbc.9.3.637
M3 - Article
C2 - 9487132
AN - SCOPUS:0031893732
SN - 1059-1524
VL - 9
SP - 637
EP - 652
JO - Molecular biology of the cell
JF - Molecular biology of the cell
IS - 3
ER -