Evidence map›Paper›PMID 17682055›Full record

ArticleMolecular and cellular biology2008

Involvement of importin-4 in the transport of transition protein 2 into the spermatid nucleus.

M M Pradeepa, S Manjunatha, V Sathish, Shipra Agrawal, M R S Rao

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 37 citations in OpenAlex.

  1. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. The roles of microRNAs in regulation of mammalian spermatogenesis.Journal of animal science and biotechnology · 2017
    Review
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  7. Article
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  12. 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

5 authors at 1 institution in 1 country.

M M PradeepaJawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560064, India.
S Manjunatha
V Sathish
Shipra Agrawal
M R S Rao
Jawaharlal Nehru Centre for Advanced Scientific Research · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian spermiogenesis is characterized by a unique chromatin-remodeling process in which histones are replaced by transition protein 1 (TP1), TP2, and TP4, which are further replaced by protamines. We showed previously that the import of TP2 into the haploid spermatid nucleus requires the components of cytosol and ATP. We have now carried out a detailed analysis to characterize the molecular components underlying the nuclear translocation of TP2. Real-time PCR analysis of the expression of different importins in testicular germ cells revealed that importin-4 and importin-beta3 are significantly up-regulated in tetraploid and haploid germ cells. We carried out physical interaction studies as well as an in vitro nuclear transport assay using recombinant TP2 and the nuclear localization signal of TP2 (TP2(NLS)) fused to glutathione S-transferase in digitonin-permeabilized, haploid, round spermatids and identified importin-4 to be involved in the import of TP2. A three-dimensional model of the importin-4 protein was generated using the crystal structure of importin-beta1 as the template. Molecular docking simulations of TP2(NLS) with the importin-4 structure led to the identification of a TP2(NLS) binding pocket spanning the three helices (helices 21 to 23) of importin-4, which was experimentally confirmed by in vitro interaction and import studies with different deletion mutants of importin-4. In contrast to TP2, TP1 import was accomplished through a passive diffusion process.

Indexed as

AnimalsBinding SitesCell NucleusChromosomal Proteins, Non-HistoneGene Expression ProfilingHumansKaryopherinsMaleMiceModels, MolecularNuclear Localization SignalsProtein BindingProtein TransportRatsRats, WistarRecombinant Fusion ProteinsChromosomal Proteins, Non-Histoneimportin 4, mouseKaryopherinsNuclear Localization SignalsRecombinant Fusion Proteinsspermatid transition proteins

Identifiers

PMID17682055
PMCPMC2447153
OpenAlexW2163780807

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.