Evidence map›Paper›PMID 16027220›Full record

ArticleThe Journal of cell biology2005

The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly.

Mario Niepel, Caterina Strambio-de-Castillia, Joseph Fasolo, Brian T Chait, Michael P Rout

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

65 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. 3D genomics and its applications in precision medicine.Cellular & molecular biology letters · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Co-Immunoprecipitation-Blotting: Analysis of Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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.

Mario NiepelThe Rockefeller University, New York, NY 10021, USA.
Caterina Strambio-de-Castillia
Joseph Fasolo
Brian T Chait
Michael P Rout
Rockefeller University · US

Funding

YNG1 PHD BINDING TO H3 3METHYL AT K4 PROMOTES TRANSCRIPTION AT TARGETED ORFSP41RR000862 · NCRR · ROCKEFELLER UNIVERSITY · PI DARNELL, JAMES E · 1985 to 2011
$16.1M
DISSECTING THE MOLECULAR MACHINERY OF NUCLEAR TRANSPORTR01GM062427 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2001 to 2010
$2.7M
COMPREHENSIVE MAP OF CELLULAR PROTEIN INTERACTIONSR33CA089810 · NCI · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2001 to 2003
$1.8M
NCI NIH HHS CA89810NCI NIH HHS R33 CA089810NCRR NIH HHS P41 RR000862NCRR NIH HHS RR00862NIGMS NIH HHS GM062427NIGMS NIH HHS R01 GM062427
6 · The paper itself

Abstract

The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their different roles within the cell. We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope-associated yeast spindle organizer. We further show that SPB function is compromised in mlp2 mutants. Cells lacking Mlp2p form significantly smaller SPBs, accumulate aberrant SPB component-containing structures inside the nucleus, and have stochastic failures of cell division. In addition, depletion of Mlp2p is synthetically lethal with mutants impaired in SPB assembly. Based on these data, we propose that Mlp2p links the SPB to the peripheral Mlp assembly, and that this linkage is required for efficient incorporation of components into the SPB.

Indexed as

Calmodulin-Binding ProteinsCell NucleusCytokinesisCytoskeletal ProteinsDNA-Directed DNA PolymeraseDNA Polymerase IMass SpectrometryMetaphaseMicroscopy, Electron, TransmissionMicrotubule-Organizing CenterMutationNuclear Pore Complex ProteinsNuclear ProteinsPhosphoproteinsProtein BindingSaccharomyces cerevisiaeCalmodulin-Binding ProteinsCytoskeletal ProteinsDNA-Directed DNA PolymeraseDNA Polymerase IMIP1 protein, S cerevisiaeMLP2 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsPhosphoproteinsSaccharomyces cerevisiae ProteinsSPC110 protein, S cerevisiaeSPC42 protein, S cerevisiae

Identifiers

PMID16027220
PMCPMC2171418
OpenAlexW2131506546

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.