Evidence map›Paper›PMID 12808039›Full record

ArticleMolecular biology of the cell2003

Golgi localization of Syne-1.

Lisa Lucio Gough, Jun Fan, Stephen Chu, Shawn Winnick, Kenneth A Beck

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Review
  3. Cells · 2021
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  7. Article
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Nesprins: from the nuclear envelope and beyond.Expert reviews in molecular medicine · 2013
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
    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

5 authors at 1 institution in 1 country.

Lisa Lucio GoughDepartment of Cell Biology and Human Anatomy, University of California, Davis, 95616, USA.
Jun Fan
Stephen Chu
Shawn Winnick
Kenneth A Beck
University of California, Davis · US

Funding

STRUCTURE/FUNCTION OF THE GOLGI MEMBRANE SKELETONR01GM059353 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI BECK, KENNETH A · 1999 to 2003
$626k
NIGMS NIH HHS GM-59353-02NIGMS NIH HHS R01 GM059353
6 · The paper itself

Abstract

We have previously identified a Golgi-localized spectrin isoform by using an antibody to the beta-subunit of erythrocyte spectrin. In this study, we show that a screen of a lambdagt11 expression library resulted in the isolation of an approximately 5-kb partial cDNA from a Madin-Darby bovine kidney (MDBK) cell line, which encoded a polypeptide of 1697 amino acids with low, but detectable, sequence homology to spectrin (37%). A blast search revealed that this clone overlaps with the 5' end of a recently identified spectrin family member Syne-1B/Nesprin-1beta, an alternately transcribed gene with muscle-specific forms that bind acetylcholine receptor and associate with the nuclear envelope. By comparing the sequence of the MDBK clone with sequence data from the human genome database, we have determined that this cDNA represents a central portion of a very large gene ( approximately 500 kb), encoding an approximately 25-kb transcript that we refer to as Syne-1. Syne-1 encodes a large polypeptide (8406 amino acids) with multiple spectrin repeats and a region at its amino terminus with high homology to the actin binding domains of conventional spectrins. Golgi localization for this spectrin-like protein was demonstrated by expression of epitope-tagged fragments in MDBK and COS cells, identifying two distinct Golgi binding sites, and by immunofluorescence microscopy by using several different antibody preparations. One of the Golgi binding domains on Syne-1 acts as a dominant negative inhibitor that alters the structure of the Golgi complex, which collapses into a condensed structure near the centrosome in transfected epithelial cells. We conclude that the Syne-1 gene is expressed in a variety of forms that are multifunctional and are capable of functioning at both the Golgi and the nuclear envelope, perhaps linking the two organelles during muscle differentiation.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesCattleCytoskeletal ProteinsDogsFluorescent Antibody TechniqueGolgi ApparatusHumansMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsProtein Structure, TertiaryCytoskeletal ProteinsNerve Tissue ProteinsNuclear ProteinsSYNE1 protein, human

Identifiers

PMID12808039
PMCPMC194889
OpenAlexW1976385869

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.