Evidence map›Paper›PMID 11877380›Full record

ArticleGenes & development2002

Calcineurin-dependent regulation of Crz1p nuclear export requires Msn5p and a conserved calcineurin docking site.

Leila M Boustany, Martha S Cyert

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed, 116 citations in OpenAlex.

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  15. Short linear motifs - ex nihilo evolution of protein regulation.Cell communication and signaling : CCS · 2015
    Review
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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

2 authors at 1 institution in 1 country.

Leila M BoustanyDepartment of Biological Sciences, Stanford University, Stanford, California 94305-5020, USA.
Martha S Cyert
Stanford University · US

Funding

Supplement to Enhance Wellness and Resiliency in the Graduate EnvironmentT32GM007276 · NIGMS · STANFORD UNIVERSITY · PI MORRISON, ASHBY J. · 1985 to 2023
$32.9M
YEAST PP2B PHOSPHATASES--ROLE IN PHEROMONE ADAPTATIONR01GM048729 · NIGMS · STANFORD UNIVERSITY · PI CYERT, MARTHA S. · 1993 to 2013
$5.4M
NIGMS NIH HHS 5T32GM07276NIGMS NIH HHS GM-48729NIGMS NIH HHS R01 GM048729NIGMS NIH HHS T32 GM007276
6 · The paper itself

Abstract

Calcineurin, a conserved Ca(2+)/calmodulin-regulated protein phosphatase, plays a crucial role in Ca(2+) signaling in a wide variety of cell types. In Saccharomyces cerevisiae, calcineurin positively regulates transcription in response to stress by dephosphorylating the transcription factor Crz1p/Tcn1p. Dephosphorylation promotes Crz1p nuclear localization in part by increasing the efficiency of its nuclear import. In this work, we show that calcineurin-dependent dephosphorylation of Crz1p also down-regulates its nuclear export. Using a genetic approach, we identify Msn5p as the exportin for Crz1p. In addition, we define the Crz1p nuclear export signal (NES) and show that it interacts with Msn5p in a phosphorylation-dependent manner. This indicates that calcineurin regulates Crz1p nuclear export by dephosphorylating and inactivating its NES. Finally, we define a motif in Crz1p, PIISIQ, similar to the PxIxIT docking site for calcineurin on the mammalian transcription factor NFAT, that mediates the in vivo interaction between calcineurin and Crz1p and is required for calcineurin-dependent regulation of Crz1p nuclear export and activity. Therefore, in yeast as in mammals, a docking site is required to target calcineurin to its substrate such that it can dephosphorylate it efficiently.

Indexed as

KaryopherinsSaccharomyces cerevisiae ProteinsActive Transport, Cell NucleusAmino Acid MotifsBinding SitesCalcineurinCarrier ProteinsCell NucleusConserved SequenceDNA-Binding ProteinsMutationProtein BindingProtein Sorting SignalsSaccharomyces cerevisiaeSequence DeletionTrans-ActivatorsCalcineurinCarrier ProteinsCRZ1 protein, S cerevisiaeDNA-Binding ProteinsKaryopherinsMSN5 protein, S cerevisiaeProtein Sorting SignalsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID11877380
PMCPMC155349
OpenAlexW2110510554

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.