Evidence map›Paper›PMID 24743598›Full record

ArticleMolecular biology of the cell2014

Α-tubulin K40 acetylation is required for contact inhibition of proliferation and cell-substrate adhesion.

Andrea Aguilar, Lars Becker, Thomas Tedeschi, Stefan Heller, Carlo Iomini, Maxence V Nachury

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.6field-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

51 citing papers in PubMed, 88 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.

Andrea AguilarDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.
Lars BeckerDepartment of Otolaryngology-Head and Neck Surgery, Stanford University School of Medicine, Stanford, CA 94305.
Thomas TedeschiDepartments of Ophthalmology and of Developmental and Regenerative Biology, Friedman Brain Institute, Mount Sinai School of Medicine, New York, NY 10029.
Stefan HellerDepartment of Otolaryngology-Head and Neck Surgery, Stanford University School of Medicine, Stanford, CA 94305.
Carlo IominiDepartments of Ophthalmology and of Developmental and Regenerative Biology, Friedman Brain Institute, Mount Sinai School of Medicine, New York, NY 10029.
Maxence V NachuryDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305 nachury@stanford.edu.
Stanford University · USAllen Institute for Brain Science · USIcahn School of Medicine at Mount Sinai · US

Funding

Quality control of the primary cilium proteomeR01GM089933 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Maxence V Nachury · 2010 to 2026
$5.8M
Stanford OHNS Core CenterP30DC010363 · NIDCD · STANFORD UNIVERSITY · PI RICCI, ANTHONY J · 2009 to 2016
$3.0M
Role of primary cilia in corneal development and repairR01EY022639 · NEI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI IOMINI, CARLO · 2012 to 2016
$2.1M
NEI NIH HHS EY022639NEI NIH HHS R01 EY022639NIDCD NIH HHS DC010363NIDCD NIH HHS P30 DC010363NIGMS NIH HHS GM089933NIGMS NIH HHS R01 GM089933
6 · The paper itself

Abstract

Acetylation of α-tubulin on lysine 40 marks long-lived microtubules in structures such as axons and cilia, and yet the physiological role of α-tubulin K40 acetylation is elusive. Although genetic ablation of the α-tubulin K40 acetyltransferase αTat1 in mice did not lead to detectable phenotypes in the developing animals, contact inhibition of proliferation and cell-substrate adhesion were significantly compromised in cultured αTat1(-/-) fibroblasts. First, αTat1(-/-) fibroblasts kept proliferating beyond the confluent monolayer stage. Congruently, αTat1(-/-) cells failed to activate Hippo signaling in response to increased cell density, and the microtubule association of the Hippo regulator Merlin was disrupted. Second, αTat1(-/-) cells contained very few focal adhesions, and their ability to adhere to growth surfaces was greatly impaired. Whereas the catalytic activity of αTAT1 was dispensable for monolayer formation, it was necessary for cell adhesion and restrained cell proliferation and activation of the Hippo pathway at elevated cell density. Because α-tubulin K40 acetylation is largely eliminated by deletion of αTAT1, we propose that acetylated microtubules regulate contact inhibition of proliferation through the Hippo pathway.

Indexed as

Cell ProliferationProtein Processing, Post-TranslationalAcetylationAcetyltransferasesAnimalsBrainCell AdhesionCells, CulturedFemaleHippo Signaling PathwayMaleMice, Inbred C57BLMice, KnockoutMicrotubule ProteinsMicrotubulesNeurofibromin 2AcetyltransferasesATAT1 protein, mouseMicrotubule ProteinsNeurofibromin 2Protein Serine-Threonine KinasesTubulin

Identifiers

PMID24743598
PMCPMC4055265
OpenAlexW2133302149

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.