Cited by 147Microtubule and mitosis dynamicsCellular transport and secretionNuclear Structure and Function

Cargo binding and regulatory sites in the tail of fungal conventional kinesin

Seiler, Stephan, Kirchner, Jochen, Horn, Christian, Kallipolitou, Athina, Woehlke, Günther, Schliwa, Manfred·2000·Nature Cell Biology

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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Crossref · 10.1038/35014022

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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).”

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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
Venue
Nature Cell Biology
Published
2000-05-09
Volume
2
Issue
6
Pages
333-338
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
OpenAlex
W1481640083
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
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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