Evidence map›Paper›PMID 27105117›Full record

ArticleMolecular cell2016

Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.

Dimitra Keramisanou, Adam Aboalroub, Ziming Zhang, Wenjun Liu, Devon Marshall, Andrea Diviney, Randy W Larsen, Ralf Landgraf, Ioannis Gelis

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 90 citations in OpenAlex.

  1. Dismissing the Chaperone in the Diabetic Kidney.Journal of the American Society of Nephrology : JASN · 2026
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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

9 authors at 3 institutions in 1 country.

Dimitra KeramisanouDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Adam AboalroubDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Ziming ZhangDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Wenjun LiuDepartment of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33136, USA.
Devon MarshallDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Andrea DivineyDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Randy W LarsenDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA.
Ralf LandgrafDepartment of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33136, USA; Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, FL 33136, USA.
Ioannis GelisDepartment of Chemistry, University of South Florida, Tampa, FL 33620, USA. Electronic address: igelis@usf.edu.
University of South Florida · USSylvester Comprehensive Cancer Center · USUniversity of Miami · US

Funding

Assembly mechanism of cochaperone-kinase complexesR01GM115854 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI GELIS, IOANNIS · 2015 to 2019
$1.6M
NIGMS NIH HHS R01 GM115854
6 · The paper itself

Abstract

Despite the essential functions of Hsp90, little is known about the mechanism that controls substrate entry into its chaperone cycle. We show that the role of Cdc37 cochaperone reaches beyond that of an adaptor protein and find that it participates in the selective recruitment of only client kinases. Cdc37 recognizes kinase specificity determinants in both clients and nonclients and acts as a general kinase scanning factor. Kinase sorting within the client-to-nonclient continuum relies on the ability of Cdc37 to challenge the conformational stability of clients by locally unfolding them. This metastable conformational state has high affinity for Cdc37 and forms stable complexes through a multidomain cochaperone interface. The interaction with nonclients is not accompanied by conformational changes of the substrate and results in substrate dissociation. Collectively, Cdc37 performs a quality control of protein kinases, where induced conformational instability acts as a "flag" for Hsp90 dependence and stable cochaperone association.

Indexed as

Cell Cycle ProteinsCells, CulturedChaperoninsEnzyme StabilityHSP90 Heat-Shock ProteinsHumansPhosphorylationProtein ConformationProtein StabilityProtein UnfoldingProto-Oncogene Proteins B-rafStructure-Activity RelationshipTemperatureTransfectionBRAF protein, humanCDC37 protein, humanCell Cycle ProteinsChaperoninsHSP90 Heat-Shock ProteinsProto-Oncogene Proteins B-raf

Identifiers

PMID27105117
PMCPMC4868553
OpenAlexW2339584249

What OpenQuestion holds

Textmetadata
LicenceTDM
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.