ArticleNature communications2019
Structural determinants of microtubule minus end preference in CAMSAP CKK domains.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
- Patronin facilitates neurite remodeling via epithelial-to-neuronal signaling.Cell communication and signaling : CCS · 2026Article
- An Orthogonal Way of Writing the Tubulin Code.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Microtubule Minus-End Binding Proteins in Cancer: Advances.Diagnostics (Basel, Switzerland) · 2025Review
- Tubulin sequence divergence is associated with the use of distinct microtubule regulators.Current biology : CB · 2025Article
- Article
- Article
- Microtubule-binding domains in Katanin p80 subunit are essential for severing activity in C. elegans.The Journal of cell biology · 2024Article
- A divergent tumor overexpressed gene domain and oligomerization contribute to SPIRAL2 function in stabilizing microtubule minus ends.The Plant cell · 2024Article
- A structural and dynamic visualization of the interaction between MAP7 and microtubules.Nature communications · 2024Article
- Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations.Current opinion in structural biology · 2024Review
- An internally controlled system to study microtubule network diversification links tubulin evolution to the use of distinct microtubule regulators.bioRxiv : the preprint server for biology · 2024Article
- Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice.Current biology : CB · 2023Article
- Preference of CAMSAP3 for expanded microtubule lattice contributes to stabilization of the minus end.Life science alliance · 2023Article
- Crystal structure of the Arabidopsis SPIRAL2 C-terminal domain reveals a p80-Katanin-like domain.PloS one · 2023Article
- CAMSAP2 organizes a γ-tubulin-independent microtubule nucleation centre through phase separation.eLife · 2022Article
- A cryo-ET survey of microtubules and intracellular compartments in mammalian axons.The Journal of cell biology · 2022Article
- Non-coding ribonucleic acid-mediatedFrontiers in genetics · 2022Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- Microtubule Organization Is Essential for Maintaining Cellular Morphology and Function.Oxidative medicine and cellular longevity · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 8 institutions in 5 countries.
Funding
Abstract
CAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To critically test this idea, we compared the human CAMSAP1 CKK domain (HsCKK) with a CKK domain from Naegleria gruberi (NgCKK), which lacks minus-end specificity. Here we report near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes, which show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit different footprints on microtubules. NMR experiments show that both HsCKK and NgCKK are remarkably rigid. However, whereas NgCKK binding does not alter the microtubule architecture, HsCKK remodels its microtubule interaction site and changes the underlying polymer structure because the tubulin lattice conformation is not optimal for its binding. Thus, in contrast to many MAPs, the HsCKK domain can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition.
Indexed as
Identifiers
What OpenQuestion holds
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.