Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis.
The in vivo function of the microtubule motor protein kinesin was examined in Drosophila using genetics and immunolocalization. Kinesin heavy chain mutations (khc) cause abnormal behavior and lethality. Mutant larvae exhibit loss of mobility and tactile responsiveness in the most posterior segments, followed by general paralysis and death during larval or pupal development. Adults homozygous for a temperature-sensitive allele also exhibit a loss in mobility and sensory responses. The data indicate that kinesin function is essential and suggest that kinesin has an important role in the neuromuscular system, perhaps as a motor for axonal transport. The possibility of more general cellular functions remains open, but observation of embryogenesis and morphogenesis in khc mutants suggests that mitosis and the cell cycle can proceed in spite of impaired kinesin function. Immunolocalization suggests that kinesin may have some general cellular functions but that it is not a major component of mitotic spindles.
Saxton
W M
WM
Department of Biology, Indiana University, Bloomington 47405.
Hicks
J
J
Goldstein
L S
LS
Raff
E C
EC
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000502:physiology*; D000483:Alleles; D000818:Animals; D004330:Drosophila / Q000196:embryology / Q000235:genetics*; D007150:Immunohistochemistry; D016547:Kinesins; D007814:Larva / Q000502:physiology; D008868:Microtubule Proteins / Q000235:genetics / Q000502:physiology*; D008938:Mitosis / Q000235:genetics; D009043:Motor Activity / Q000235:genetics; D009154:Mutation
D008868:Microtubule Proteins; D000251:Adenosine Triphosphatases; D016547:Kinesins