Evidence map›Paper›PMID 18443039›Full record

ArticleMolecular and cellular biology2008

Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.

Atin K Mandal, Nadinath B Nillegoda, Jennifer A Chen, Avrom J Caplan

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 30 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

4 authors at 1 institution in 1 country.

Atin K MandalDepartment of Biology, City College New York, Convent Avenue at 138th Street, New York, NY 10031, USA.
Nadinath B Nillegoda
Jennifer A Chen
Avrom J Caplan
Icahn School of Medicine at Mount Sinai · US

Funding

Hsp90 Chaperone Machine Structure and FunctionR01GM070596 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI CAPLAN, AVROM J. · 2005 to 2009
$1.2M
NIGMS NIH HHS GM70596NIGMS NIH HHS R01 GM070596
6 · The paper itself

Abstract

Ydj1 is a Saccharomyces cerevisiae Hsp40 molecular chaperone that functions with Hsp70 to promote polypeptide folding. We identified Ydj1 as being important for maintaining steady-state levels of protein kinases after screening several chaperones and cochaperones in gene deletion mutant strains. Pulse-chase analyses revealed that a portion of Tpk2 kinase was degraded shortly after synthesis in a ydj1Delta mutant, while the remainder was capable of maturing but with reduced kinetics compared to the wild type. Cdc28 maturation was also delayed in the ydj1Delta mutant strain. Ydj1 protects nascent kinases in different contexts, such as when Hsp90 is inhibited with geldanamycin or when CDC37 is mutated. The protective function of Ydj1 is due partly to its intrinsic chaperone function, but this is minor compared to the protective effect resulting from its interaction with Hsp70. SIS1, a type II Hsp40, was unable to suppress defects in kinase accumulation in the ydj1Delta mutant, suggesting some specificity in Ydj1 chaperone action. However, analysis of chimeric proteins that contained the chaperone modules of Ydj1 or Sis1 indicated that Ydj1 promotes kinase accumulation independently of its client-binding specificity. Our results suggest that Ydj1 can both protect nascent chains against degradation and control the rate of kinase maturation.

Indexed as

Protein Processing, Post-TranslationalCDC28 Protein Kinase, S cerevisiaeCell Cycle ProteinsCyclic AMP-Dependent Protein KinasesEnzyme StabilityGene DeletionHSP40 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesMutationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityCDC28 Protein Kinase, S cerevisiaeCDC37 protein, S cerevisiaeCell Cycle ProteinsCyclic AMP-Dependent Protein KinasesHSP40 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesProtein KinasesSaccharomyces cerevisiae ProteinsTPK2 protein, S cerevisiaeYDJ1 protein, S cerevisiae

Identifiers

PMID18443039
PMCPMC2447146
OpenAlexW2110913873

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.