Evidence map›Paper›PMID 19929865›Full record

ArticleTraffic (Copenhagen, Denmark)2010

Nap1 and Chz1 have separate Htz1 nuclear import and assembly functions.

Korinna Straube, Jeffrey S Blackwell, Lucy F Pemberton

Open access · greenAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 52 citations in OpenAlex.

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  8. Review
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  13. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
  14. Article
  15. Review
  16. Review
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  18. Article
  19. Histone chaperones in nucleosome assembly and human disease.Nature structural & molecular biology · 2013
    Review
  20. Article
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

3 authors at 1 institution in 1 country.

Korinna StraubeCenter for Cell Signaling, Department of Microbiology, University of Virginia Health Sciences Center, University of Virginia, Charlottesville, VA 22908, USA.
Jeffrey S Blackwell
Lucy F Pemberton
University of Virginia · US

Funding

HISTONE NUCLEAR IMPORT AND CHROMATIN ASSEMBLYR01GM065385 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PEMBERTON, LUCY F · 2002 to 2010
$2.7M
NIGMS NIH HHS GM065385NIGMS NIH HHS R01 GM065385
6 · The paper itself

Abstract

We analyzed the nuclear import and regulation of the yeast histone variant Htz1 (H2A.Z), and the role of histone chaperones Nap1 and Chz1 in this process. Copurification suggested that Htz1 and H2B dimerized in the cytoplasm prior to import. Like H2B, Htz1 contained a nuclear localization signal (NLS) in its N-terminus that is recognized by multiple karyopherins (also called importins), indicating multiple transport pathways into the nucleus. However, Kap114 and Kap123 appeared to play the major role in Htz1 import. We also identified a role for Nap1 in the import of Htz1/H2B heterodimers, and Nap1 formed a RanGTP-insensitive import complex with Htz1/H2B and Kap114. Nap1 was necessary for maintaining a soluble pool of Htz1, indicating that its chaperone function may be important for the dynamic exchange of histones within nucleosomes. In contrast, Chz1 was imported by a distinct import pathway, and Chz1 did not appear to interact with Htz1 in the cytoplasm. Genetic analysis indicated that NAP1 has a function in the absence of HTZ1 that is not shared with CHZ1. This provides further evidence that the histone chaperones Nap1 and Chz1 have separate Htz1-dependent and -independent functions.

Indexed as

Active Transport, Cell NucleusCell Cycle ProteinsCell NucleusCytoskeletal ProteinsCytosolHistone ChaperonesHistonesKaryopherinsNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionCell Cycle ProteinsChz1 protein, S cerevisiaeCytoskeletal ProteinsHistone ChaperonesHistonesHtz1 protein, S cerevisiaeKaryopherinsNBP1 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19929865
PMCPMC2907061
OpenAlexW2092300172

What OpenQuestion holds

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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.