ArticleBiophysical reviews2013
Intrinsic Disorder in the Kinesin Superfamily.
Article in Biophysical reviews, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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
16 citing papers in PubMed, 24 citations in OpenAlex.
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance.Nature reviews. Molecular cell biology · 2026Review
- An atlas of RNA-dependent proteins in cell division reveals the riboregulation of mitotic protein-protein interactions.Nature communications · 2025Article
- The kinesin-3 KIF1C undergoes liquid-liquid phase separation for accumulation of specific transcripts at the cell periphery.The EMBO journal · 2024Article
- A kinesin-13 family kinesin in Trypanosoma brucei regulates cytokinesis and cytoskeleton morphogenesis by promoting microtubule bundling.PLoS pathogens · 2024Article
- ALS-linked KIF5A ΔExon27 mutant causes neuronal toxicity through gain-of-function.EMBO reports · 2022Article
- ELK1-induced up-regulation of KIF26B promotes cell cycle progression in breast cancer.Medical oncology (Northwood, London, England) · 2021Article
- Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding.Science advances · 2021Article
- Molecular basis of mRNA transport by a kinesin-1-atypical tropomyosin complex.Genes & development · 2021Article
- The adaptor proteins HAP1a and GRIP1 collaborate to activate the kinesin-1 isoform KIF5C.Journal of cell science · 2019Article
- Plant Kinesin-12: Localization Heterogeneity and Functional Implications.International journal of molecular sciences · 2019Review
- Article
- SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain.Journal of cell science · 2017Article
- FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination.The Journal of cell biology · 2017Article
- Condensin I-mediated mitotic chromosome assembly requires association with chromokinesin KIF4A.Genes & development · 2016Article
- Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013).Intrinsically disordered proteins · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kinesin molecular motors perform a myriad of intracellular transport functions. While their mechanochemical mechanisms are well understood and well-conserved throughout the superfamily, the cargo-binding and regulatory mechanisms governing the activity of kinesins are highly diverse and in general, are incompletely characterized. Here we present evidence from bioinformatic predictions indicating that most kinesin superfamily members contain significant regions of intrinsically disordered (ID) residues. ID regions can bind to multiple partners with high specificity, and are highly labile to post-translational modification and degradation signals. In kinesins, the predicted ID regions are primarily found in areas outside the motor domains, where primary sequences diverge by family, suggesting that ID may be a critical structural element for determining the functional specificity of individual kinesins. To support this idea, we present a systematic analysis of the kinesin superfamily, family by family, for predicted regions of ID. We combine this analysis with a comprehensive review of kinesin binding partners and post-translational modifications. We find two key trends across the entire kinesin superfamily. First, ID residues tend to be in the tail regions of kinesins, opposite the superfamily-conserved motor domains. Second, predicted ID regions correlate to regions that are known to bind to cargoes and/or undergo post-translational modifications. We therefore propose that ID is a structural element utilized by the kinesin superfamily in order to impart functional specificity to individual kinesins.
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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.