Evidence map›Paper›PMID 24706919›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin.

Melissa C Hendershott, Ronald D Vale

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
6.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

104 citing papers in PubMed, 168 citations in OpenAlex.

  1. Article
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  7. Microtubule Minus-End Binding Proteins in Cancer: Advances.Diagnostics (Basel, Switzerland) · 2025
    Review
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44 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Melissa C HendershottDepartment of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, CA 94158.
Ronald D Vale
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

GENETICS OF EUCARYOTIC AND PROCARYOTIC ORGANISMST32GM007810 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ASHRAFI, KAVEH, NARLIKAR, GEETA J · 1985 to 2020
$15.1M
Microtubule Complexes Involved in Intracelluar TransportR37GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2006 to 2015
$3.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R37 GM038499NIGMS NIH HHS T32 GM007810PHS HHS 38499
6 · The paper itself

Abstract

The microtubule (MT) cytoskeleton plays an essential role in mitosis, intracellular transport, cell shape, and cell migration. The assembly and disassembly of MTs, which can occur through the addition or loss of subunits at the plus- or minus-ends of the polymer, is essential for MTs to carry out their biological functions. A variety of proteins act on MT ends to regulate their dynamics, including a recently described family of MT minus-end binding proteins called calmodulin-regulated spectrin-associated protein (CAMSAP)/Patronin/Nezha. Patronin, the single member of this family in Drosophila, was previously shown to stabilize MT minus-ends against depolymerization in vitro and in vivo. Here, we show that all three mammalian CAMSAP family members also bind specifically to MT minus-ends and protect them against kinesin-13-induced depolymerization. However, these proteins differ in their abilities to suppress tubulin addition at minus-ends and to dissociate from MTs. CAMSAP1 does not interfere with polymerization and tracks along growing minus-ends. CAMSAP2 and CAMSAP3 decrease the rate of tubulin incorporation and remain bound, thereby creating stretches of decorated MT minus-ends. By using truncation analysis, we find that somewhat different minimal domains of CAMSAP and Patronin are involved in minus-end localization. However, we find that, in both cases, a highly conserved C-terminal domain and a more variable central domain cooperate to suppress minus-end dynamics in vitro and that both regions are required to stabilize minus-ends in Drosophila S2 cells. These results show that members of the CAMSAP/Patronin family all localize to and protect minus-ends but have evolved distinct effects on MT dynamics.

Indexed as

AnimalsCytoskeletal ProteinsDrosophila melanogasterDrosophila ProteinsHumansKinesinsMicrotubule-Associated ProteinsMicrotubulesPolymerizationProtein BindingProtein Structure, TertiaryProtein SubunitsTubulinCAMSAP1 protein, humanCAMSAP2 protein, humanCamsap3 protein, mouseCytoskeletal ProteinsDrosophila ProteinsKinesinsMicrotubule-Associated Proteinspatronin protein, DrosophilaProtein SubunitsTubulincytoskeletal regulationTIRF microscopytubulin polymerization

Identifiers

PMID24706919
PMCPMC4000804
OpenAlexW2060504185

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.