ArticleThe Journal of cell biology1996
Sequence and submolecular localization of the 115-kD accessory subunit of the heterotrimeric kinesin-II (KRP85/95) complex.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
69 citing papers in PubMed.
- Heterotrimeric kinesin-2 autoinhibition mediated by interactions of the CC2 and proximal tail domains with the motor domains is essential for cilium formation and maintenance.bioRxiv : the preprint server for biology · 2026Article
- Joubert syndrome 26 protein enforces compartmentalized motility of a ciliary kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Kinesins inOpen biology · 2025Review
- Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025Article
- A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport.Nature communications · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- The two-step cargo recognition mechanism of heterotrimeric kinesin.EMBO reports · 2023Article
- KAP is the neuronal organelle adaptor for Kinesin-2 KIF3AB and KIF3AC.Molecular biology of the cell · 2022Article
- Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport.Frontiers in cell and developmental biology · 2022Review
- Direct imaging of intraflagellar-transport turnarounds reveals that motors detach, diffuse, and reattach to opposite-direction trains.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020Review
- Kinesin-2 from C. reinhardtii Is an Atypically Fast and Auto-inhibited Motor that Is Activated by Heterotrimerization for Intraflagellar Transport.Current biology : CB · 2020Article
- The crowding dynamics of the motor protein kinesin-II.PloS one · 2020Article
- Kinesin-2 heterodimerization alters entry into a processive run along the microtubule but not stepping within the run.The Journal of biological chemistry · 2018Article
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
- Intraflagellar transport: mechanisms of motor action, cooperation, and cargo delivery.The FEBS journal · 2017Review
- Intraflagellar transport velocity is governed by the number of active KIF17 and KIF3AB motors and their motility properties under load.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run.The Journal of biological chemistry · 2016Article
- Fast or Slow, Either Head Can Start the Processive Run of Kinesin-2 KIF3AC.The Journal of biological chemistry · 2016Article
- Functional differentiation of cooperating kinesin-2 motors orchestrates cargo import and transport in C. elegans cilia.Nature cell biology · 2015Article
9 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
The heterotrimeric kinesin-II holoenzyme purified from sea urchin (Strongylocentrotus purpuratus) eggs is assembled from two heterodimerized kinesin-related motor subunits of known sequence, together with a third, previously uncharacterized 115-kD subunit, SpKAP115. Using monospecific anti-SpKAP115 antibodies we have accomplished the molecular cloning and sequencing of the SpKAP115 subunit. The deduced sequence predicts a globular 95-kD non-motor "accessory" polypeptide rich in alpha-helical segments that are generally not predicted to form coiled coils. Electron microscopy of individual rotary shadowed kinesin-II holoenzymes also suggests that SpKAP115 is globular, with a somewhat asymmetric morphology. Moreover, the SpKAP115 subunit lies at one end of the 51-nm-long kinesin-II complex, being separated from the two presumptive motor domains by a approximately 26-nm-long rod, in a manner similar to the light chains (KLCs) of kinesin itself. This indicates that SpKAP115 and the KLCs may have analogous functions, yet SpKAP115 does not display significant sequence similarity with the KLCs. The results show that kinesin and kinesin-II are assembled from highly divergent accessory polypeptides together with kinesin related motor subunits (KRPs) containing conserved motor domains linked to divergent tails. Despite the lack of sequence conservation outside the motor domains, there is striking conservation of the ultrastructure of the kinesin and kinesin-II holoenzymes.
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