Evidence map›Paper›PMID 18086883›Full record

ArticleMolecular and cellular biology2008

Phosphorylation by casein kinase 2 regulates Nap1 localization and function.

Meredith E K Calvert, Kristin M Keck, Celeste Ptak, Jeffrey Shabanowitz, Donald F Hunt, Lucy F Pemberton

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

24 citing papers in PubMed, 38 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 2 institutions in 2 countries.

Meredith E K CalvertCenter for Cell Signaling, University of Virginia, Box 800577 HSC, Charlottesville, VA 22908, USA.
Kristin M Keck
Celeste Ptak
Jeffrey Shabanowitz
Donald F Hunt
Lucy F Pemberton
Toxicologie, Pharmacologie et Signalisation Cellulaire · FRUniversity of Virginia · US

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
TRAINING IN CELL AND MOLECULAR BIOLOGYT32GM008136 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI STUKENBERG, P. TODD · 1985 to 2020
$8.5M
HISTONE NUCLEAR IMPORT AND CHROMATIN ASSEMBLYR01GM065385 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PEMBERTON, LUCY F · 2002 to 2010
$2.7M
NIGMS NIH HHS R01 GM037537NIGMS NIH HHS R01 GM065385NIGMS NIH HHS R01 GM65385NIGMS NIH HHS T32 GM008136
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and identified by mass spectrometry. We identified several kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated protein, Nba1. Consistent with our identification of the Nap1-interacting kinases, we showed that Nap1 is phosphorylated in vivo at 11 sites and that Nap1 is phosphorylated by CK2 at three substrate serines. Phosphorylation of these serines was not necessary for normal bud formation, but mutation of these serines to either alanine or aspartic acid resulted in cell cycle changes, including a prolonged S phase, suggesting that reversible phosphorylation by CK2 is important for cell cycle regulation. Nap1 can shuttle between the nucleus and cytoplasm, and we also showed that CK2 phosphorylation promotes the import of Nap1 into the nucleus. In conclusion, our data show that Nap1 phosphorylation by CK2 appears to regulate Nap1 localization and is required for normal progression through S phase.

Indexed as

Active Transport, Cell NucleusCasein Kinase IICell CycleCell Cycle ProteinsCell NucleusCyclin BHistonesNuclear ProteinsNucleosome Assembly Protein 1PhosphoproteinsPhosphorylationProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCasein Kinase IICell Cycle ProteinsCLB2 protein, S cerevisiaeCyclin BHistonesNAP1 protein, S cerevisiaeNuclear ProteinsNucleosome Assembly Protein 1PhosphoproteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID18086883
PMCPMC2258750
OpenAlexW2168182432

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.