Cited by 201Microtubule and mitosis dynamicsNeurobiology and Insect Physiology ResearchDevelopmental Biology and Gene Regulation

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Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis

Saxton, William M., Hicks, Jennifer, Goldstein, Lawrence S.B., Raff, Elizabeth C.·1991·Cell

DOI 10.1016/0092-8674(91)90264-y

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Abstract

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.

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Authors: Saxton, W. M., Hicks, J., Goldstein, L. S. B., & Raff, E. C.
Affiliations: Indiana University Bloomington (US)
Harvard University (US)
ORCID: Goldstein, Lawrence S.B.
Venue: Cell
Publisher: Elsevier BV
Published: 1991-03
Volume: 64
Issue: 6
Pages: 1093-1102
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(91)90264-y
OpenAlex: W1996061686
Cited by: 201
References: 41
Citations by year: 2025: 4 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 6 · 2013: 5 · 2012: 10
FWCI: 7.67
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hd016739-13)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 16739)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurobiology and Insect Physiology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords: kinesin heavy chain, microtubule motor proteins, Drosophila, lethality, neuromuscular function, axonal transport, mitosis, mitotic spindle, embryonic development, morphogenesis, temperature-sensitive mutants, larval locomotion, sensory responses
MeSH terms: Adenosine Triphosphatases, Alleles, Animals, Drosophila, Immunohistochemistry, Larva, Microtubule Proteins, Mitosis, Motor Activity, Mutation, Kinesins

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Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis

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