Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis
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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Kinesin-I plays a primary role in neuronal transport.
“Previous studies with mutants lacking KHC in invertebrate organisms have all given neuronal phenotypes (Saxton et al. 1991; Gho et al. 1992; Patel et al. 1993; Hurd and Saxton 1996), suggesting that kinesin-I plays a primary role in neuronal transport.”
From Defective kinesin heavy chain behavior in mouse kinesin light chain mutants (1999) · cites this paper as Saxton et al. 1991
Kinesin is required for axonal transport in neuronal cells.
“Genetic studies in Caenorhabditis elegans, Drosophila melanogaster, and mice have failed to identify the primary cargo of conventional kinesin although, they have demonstrated that kinesin is required for axonal transport in neuronal cells (Saxton et al. 1991; Gho et al. 1992; Patel et al. 1993; Hurd and Saxton 1996; Hurd et al. 1996; Gindhart et al. 1998; Tanaka et al. 1998; Rahman et al. 1999).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Saxton et al. 1991
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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)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1991-03
- Volume
- 64
- Issue
- 6
- Pages
- 1093-1102
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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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