ArticleCurrent biology : CB2011
Kif18A uses a microtubule binding site in the tail for plus-end localization and spindle length regulation.
Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 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
73 citing papers in PubMed, 114 citations in OpenAlex.
- KIF18A inhibitor prevents chromosomally unstable osteosarcoma growth by activating spindle assembly checkpoint.Cancer biology & therapy · 2026Article
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- Kinesins inOpen biology · 2025Review
- The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding.Molecular biology of the cell · 2025Article
- KIF18A inhibition: the next big player in the search for cancer therapeutics.Cancer metastasis reviews · 2024Review
- HURP regulates Kif18A recruitment and activity to synergistically control microtubule dynamics.Nature communications · 2024Article
- Spermatocytes have the capacity to segregate chromosomes despite centriole duplication failure.EMBO reports · 2024Article
- Molecular interplay between HURP and Kif18A in mitotic spindle regulation.Research square · 2024Article
- Modification of the neck-linker of KIF18A alters Microtubule subpopulation preference.Molecular biology of the cell · 2024Article
- Importin α/β promote Kif18B microtubule association and enhance microtubule destabilization activity.Molecular biology of the cell · 2023Article
- Kinesins Modify ERR1-Dependent Transcription Using a Conserved Nuclear Receptor Box Motif.International journal of molecular sciences · 2023Article
- BAP1 loss induces mitotic defects in mesothelioma cells through BRCA1-dependent and independent mechanisms.Oncogene · 2023Article
- Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape.Nature communications · 2022Article
- Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022Review
- Integrated bioinformatics analysis to identify key genes related to the prognosis of esophageal squamous cell carcinoma.Translational cancer research · 2021Article
- Article
- Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion.Communications biology · 2021Article
- Review
- Selective and ATP-competitive kinesin KIF18A inhibitor suppresses the replication of influenza A virus.Journal of cellular and molecular medicine · 2020Article
- Kinesin family member KIF18A is a critical cellular factor that regulates the differentiation and activation of dendritic cells.Genes & genomics · 2020Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The mitotic spindle is a macromolecular structure utilized to properly align and segregate sister chromatids to two daughter cells. During mitosis, the spindle maintains a constant length, even though the spindle microtubules (MTs) are constantly undergoing polymerization and depolymerization [1]. Members of the kinesin-8 family are important for the regulation of spindle length and for chromosome positioning [2-9]. Kinesin-8 proteins are length-specific, plus-end-directed motors that are proposed to be either MT depolymerases [3, 4, 8, 10, 11] or MT capping proteins [12]. How Kif18A uses its destabilization activity to control spindle morphology is not known. We found that Kif18A controls spindle length independently of its role in chromosome positioning. The ability of Kif18A to control spindle length is mediated by an ATP-independent MT binding site at the C-terminal end of the Kif18A tail that has a strong affinity for MTs in vitro and in cells. We used computational modeling to ask how modulating the motility or binding properties of Kif18A would affect its activity. Our modeling predicts that both fast motility and a low off rate from the MT end are important for Kif18A function. In addition, our studies provide new insight into how depolymerizing and capping enzymes can lead to MT destabilization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.