Evidence map›Paper›PMID 22696680›Full record

ArticleMolecular biology of the cell2012

Fission yeast Alp14 is a dose-dependent plus end-tracking microtubule polymerase.

Jawdat Al-Bassam, Hwajin Kim, Ignacio Flor-Parra, Neeraj Lal, Hamida Velji, Fred Chang

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

57 citing papers in PubMed, 90 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Jawdat Al-BassamDepartment of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA. jawdat@ucdavis.edu
Hwajin Kim
Ignacio Flor-Parra
Neeraj Lal
Hamida Velji
Fred Chang
Columbia University · USHarvard University · USUniversity of California, Davis · US

Funding

Hormones: Molecular Mechanism of Action and FunctionsT32DK007328 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI KOUSTENI, STAVROULA · 1986 to 2025
$7.8M
Nuclear Positioning and Microtubule OrganizationR01GM069670 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CHANG, FRED · 2005 to 2012
$2.4M
Microtubule Polymerization and Depolymerization Mechanisms by Conserved ProteinsR00GM084292 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI AL-BASSAM, JAWDAT MH · 2011 to 2013
$715k
NIDDK NIH HHS DK07328NIDDK NIH HHS T32 DK007328NIGMS NIH HHS R00 GM084292NIGMS NIH HHS R01 GM069670PHS HHS R00 GMO8429
6 · The paper itself

Abstract

XMAP215/Dis1 proteins are conserved tubulin-binding TOG-domain proteins that regulate microtubule (MT) plus-end dynamics. Here we show that Alp14, a XMAP215 orthologue in fission yeast, Schizosaccharomyces pombe, has properties of a MT polymerase. In vivo, Alp14 localizes to growing MT plus ends in a manner independent of Mal3 (EB1). alp14-null mutants display short interphase MTs with twofold slower assembly rate and frequent pauses. Alp14 is a homodimer that binds a single tubulin dimer. In vitro, purified Alp14 molecules track growing MT plus ends and accelerate MT assembly threefold. TOG-domain mutants demonstrate that tubulin binding is critical for function and plus end localization. Overexpression of Alp14 or only its TOG domains causes complete MT loss in vivo, and high Alp14 concentration inhibits MT assembly in vitro. These inhibitory effects may arise from Alp14 sequestration of tubulin and effects on the MT. Our studies suggest that Alp14 regulates the polymerization state of tubulin by cycling between a tubulin dimer-bound cytoplasmic state and a MT polymerase state that promotes rapid MT assembly.

Indexed as

Microtubule-Associated ProteinsMicrotubulesSchizosaccharomyces pombe ProteinsInterphaseMutationProtein BindingSchizosaccharomycesSpindle ApparatusTubulinalp14 protein, S pombeMal3 protein, S pombeMicrotubule-Associated ProteinsSchizosaccharomyces pombe ProteinsTubulin

Identifiers

PMID22696680
PMCPMC3408415
OpenAlexW1993795982

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.