Cargo binding and regulatory sites in the tail of fungal conventional kinesin
Abstract
Here, using a quantitative in vivo assay, we map three regions in the carboxy terminus of conventional kinesin that are involved in cargo association, folding and regulation, respectively. Using C-terminal and internal deletions, point mutations, localization studies, and an engineered 'minimal' kinesin, we identify five heptads of a coiled-coil domain in the kinesin tail that are necessary and sufficient for cargo association. Mutational analysis and in vitro ATPase assays highlight a conserved motif in the globular tail that is involved in regulation of the motor domain; a region preceding this motif participates in folding. Although these sites are spatially and functionally distinct, they probably cooperate during activation of the motor for cargo transport.
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The truncated KHC protein (KHC-891) was largely found at the tips of cellular processes.
“Indeed, the truncated KHC protein was largely found at the tips of cellular processes (Fig. 5 D), consistent with its uninhibited migration towards the plus end of MTs and in agreement with similar results in COS cells (Verhey et al. 1998) and Neurospora (Seiler et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Seiler et al. 2000
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- Authors
- Seiler, S., Kirchner, J., Horn, C., Kallipolitou, A., Woehlke, G., & Schliwa, M.
- Affiliations
- Adolf-Butenandt-Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie (DE)
- Corresponding author
- Schliwa, Manfred
- ORCID
- Woehlke, Günther
- Venue
- Nature Cell Biology
- Published
- 2000-05-09
- Volume
- 2
- Issue
- 6
- Pages
- 333-338
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W1481640083
- Semantic Scholar
- 67afb86f9a3c9a012f0e51d501a82feb20c97fbc
- Cited by
- 147
- References
- 50
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 7 · 2022: 8 · 2021: 3 · 2020: 1 · 2019: 1 · 2018: 5 · 2016: 3 · 2015: 1 · 2014: 4 · 2013: 5 · 2012: 7
- FWCI
- 4.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- cargo binding, coiled-coil domain, heptad repeat, protein folding, ATPase activity, freight transport, motor activation
- MeSH terms
- Adenosine Triphosphatases, Amino Acid Sequence, Binding Sites, Fluorescent Antibody Technique, Fungal Proteins, Genetic Complementation Test, Kinetics, Molecular Sequence Data, Mutation, Neurospora, Phenotype, Recombinant Fusion Proteins, Substrate Specificity, Kinesins, Conserved Sequence, Protein Structure, Tertiary, Protein Folding, Amino Acid Substitution, Molecular Motor Proteins, Amino Acid Motifs
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