Evidence map›Paper›PMID 9531556›Full record

ArticleThe Journal of cell biology1998

Pericentrin and gamma-tubulin form a protein complex and are organized into a novel lattice at the centrosome.

J B Dictenberg, W Zimmerman, C A Sparks, A Young, C Vidair, Y Zheng, W Carrington, F S Fay, S J Doxsey

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed
12.0field-weighted citation impact, top 1% 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

201 citing papers in PubMed, 493 citations in OpenAlex.

  1. Article
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  9. Methods to Determine the Role of MIF in Cilia Biogenesis.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  10. Article
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  17. Centrosome Movements Are TUBG1-Dependent.International journal of molecular sciences · 2023
    Article
  18. Article
  19. Article
  20. Article

141 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

9 authors at 4 institutions in 1 country.

J B DictenbergProgram in Molecular Medicine and Department of Cell Biology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655, USA.
W Zimmerman
C A Sparks
A Young
C Vidair
Y Zheng
W Carrington
F S Fay
S J Doxsey
Carnegie Institution for Science · USFoundation for Biomedical Research · USUniversity of California, San Francisco · USUniversity of Massachusetts Chan Medical School · US

Funding

Mitotic functions of cilia proteinsR01GM051994 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI DOXSEY, STEPHEN J · 1995 to 2014
$4.3M
SCANNING PARTIAL CONFOCAL MICROSCOPER01RR009799 · NCRR · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CARRINGTON, WALTER A. · 1995 to 1997
–
NCRR NIH HHS R01 RR09799-01A1NIGMS NIH HHS R01 GM051994NIGMS NIH HHS R01GM51994
6 · The paper itself

Abstract

Pericentrin and gamma-tubulin are integral centrosome proteins that play a role in microtubule nucleation and organization. In this study, we examined the relationship between these proteins in the cytoplasm and at the centrosome. In extracts prepared from Xenopus eggs, the proteins were part of a large complex as demonstrated by sucrose gradient sedimentation, gel filtration and coimmunoprecipitation analysis. The pericentrin-gamma-tubulin complex was distinct from the previously described gamma-tubulin ring complex (gamma-TuRC) as purified gamma-TuRC fractions did not contain detectable pericentrin. When assembled at the centrosome, the two proteins remained in close proximity as shown by fluorescence resonance energy transfer. The three- dimensional organization of the centrosome-associated fraction of these proteins was determined using an improved immunofluorescence method. This analysis revealed a novel reticular lattice that was conserved from mammals to amphibians, and was organized independent of centrioles. The lattice changed dramatically during the cell cycle, enlarging from G1 until mitosis, then rapidly disassembling as cells exited mitosis. In cells colabeled to detect centrosomes and nucleated microtubules, lattice elements appeared to contact the minus ends of nucleated microtubules. Our results indicate that pericentrin and gamma-tubulin assemble into a unique centrosome lattice that represents the higher-order organization of microtubule nucleating sites at the centrosome.

Indexed as

AnimalsAntigensCell CycleCell FractionationCells, CulturedCentrifugation, Density GradientCentrosomeCHO CellsChromatography, GelCOS CellsCricetinaeFluorescent Antibody TechniqueMicrotubule-Associated ProteinsMicrotubulesTubulinXenopusAntigensMicrotubule-Associated ProteinspericentrinTubulin

Identifiers

PMID9531556
PMCPMC2132723
OpenAlexW2125148239

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.