Evidence map›Paper›PMID 22241783›Full record

ArticleGenes & development2012

Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization.

Laura T Donlin, Christian Andresen, Steffen Just, Eugene Rudensky, Christopher T Pappas, Martina Kruger, Erica Y Jacobs, Andreas Unger, Anke Zieseniss, Marc-Werner Dobenecker and 6 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
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

99 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
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  6. LC-MS profiling ofbioRxiv : the preprint server for biology · 2026
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39 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

16 authors at 5 institutions in 2 countries.

Laura T DonlinLaboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, New York, NY 10065, USA.
Christian Andresen
Steffen Just
Eugene Rudensky
Christopher T Pappas
Martina Kruger
Erica Y Jacobs
Andreas Unger
Anke Zieseniss
Marc-Werner Dobenecker
Tobias Voelkel
Brian T Chait
Carol C Gregorio
Wolfgang Rottbauer
Alexander Tarakhovsky
Wolfgang A Linke
Rockefeller University · USRuhr University Bochum · DEUniversität Ulm · DEUniversity of Arizona · USUniversity of Göttingen · DE

Funding

NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
YNG1 PHD BINDING TO H3 3METHYL AT K4 PROMOTES TRANSCRIPTION AT TARGETED ORFSP41RR000862 · NCRR · ROCKEFELLER UNIVERSITY · PI DARNELL, JAMES E · 1985 to 2011
$16.1M
PHYSIOLOGYT32HL007249 · NHLBI · UNIVERSITY OF ARIZONA · PI Brett A Colson, JOHN P KONHILAS · 1985 to 2026
$12.5M
Deciphering the Roles of Nebulin in Cardiac Myofibril AssemblyR01HL083146 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2007 to 2011
$2.1M
Control of T cell signaling by methyltransferase Ezh2R01AI068058 · NIAID · ROCKEFELLER UNIVERSITY · PI TARAKHOVSKY, ALEXANDER · 2007 to 2011
$2.1M
Setdb2 methyltransferase in B cell differentiationF32AI066674 · NIAID · ROCKEFELLER UNIVERSITY · PI DONLIN, LAURA T. · 2006 to 2008
$145k
Isolation and Characterization of Yeast rDNA ChromatinF32GM076989 · NIGMS · ROCKEFELLER UNIVERSITY · PI JACOBS, ERICA Y · 2006 to 2007
$95k
NCRR NIH HHS P41 RR000862NCRR NIH HHS RR00862NCRR NIH HHS RR022220NCRR NIH HHS U54 RR022220NHLBI NIH HHS HL083146NHLBI NIH HHS R01 HL083146NHLBI NIH HHS T32 HL007249NIAID NIH HHS AI066674NIAID NIH HHS F32 AI066674NIAID NIH HHS R01 AI068058NIGMS NIH HHS F32 GM076989NIGMS NIH HHS GM076989
6 · The paper itself

Abstract

Protein lysine methylation is one of the most widespread post-translational modifications in the nuclei of eukaryotic cells. Methylated lysines on histones and nonhistone proteins promote the formation of protein complexes that control gene expression and DNA replication and repair. In the cytoplasm, however, the role of lysine methylation in protein complex formation is not well established. Here we report that the cytoplasmic protein chaperone Hsp90 is methylated by the lysine methyltransferase Smyd2 in various cell types. In muscle, Hsp90 methylation contributes to the formation of a protein complex containing Smyd2, Hsp90, and the sarcomeric protein titin. Deficiency in Smyd2 results in the loss of Hsp90 methylation, impaired titin stability, and altered muscle function. Collectively, our data reveal a cytoplasmic protein network that employs lysine methylation for the maintenance and function of skeletal muscle.

Indexed as

AnimalsChick EmbryoConnectinCytoplasmHistone-Lysine N-MethyltransferaseHSP90 Heat-Shock ProteinsHumansLysineMethylationMuscle ProteinsMuscle, SkeletalMyocardiumMyofibrilsProtein KinasesRecombinant ProteinsZebrafishConnectinHistone-Lysine N-MethyltransferaseHSP90 Heat-Shock ProteinsLysineMuscle ProteinsProtein KinasesRecombinant ProteinsTTN protein, human

Identifiers

PMID22241783
PMCPMC3273835
OpenAlexW2124471305

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.