Evidence map›Paper›PMID 18764929›Full record

ArticleTraffic (Copenhagen, Denmark)2008

Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins.

Maria Luisa Oppizzi, Armin Akhavan, Manisha Singh, Jimmie E Fata, John L Muschler

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Laminin-dystroglycan signaling regulates retinal arteriogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  10. Article
  11. γ-Secretase Dependent Nuclear Targeting of Dystroglycan.Journal of cellular biochemistry · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Post-translational regulation of signaling mucins.Current opinion in structural biology · 2011
    Review
  20. Basement membranes: cell scaffoldings and signaling platforms.Cold Spring Harbor perspectives in biology · 2011
    Review
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 2 institutions in 1 country.

Maria Luisa OppizziCalifornia Pacific Medical Center Research Institute, 475 Brannan Street, Suite 220, San Francisco, CA 94107, USA.
Armin Akhavan
Manisha Singh
Jimmie E Fata
John L Muschler
California Pacific Medical Center · USCity University of New York · US

Funding

Dystroglycan in Epithelial Architecture and FunctionR01CA109579 · NCI · CALIFORNIA PACIFIC MED CTR RES INSTITUTE · PI MUSCHLER, JOHN L · 2005 to 2009
$1.6M
NCI NIH HHS R01 CA109579
6 · The paper itself

Abstract

Dystroglycan (DG) is an extracellular matrix receptor implicated in muscular dystrophies and cancers. DG belongs to the membrane-tethered mucin family and is composed of extracellular (alpha-DG) and transmembrane (beta-DG) subunits stably coupled at the cell surface. These two subunits are generated by autoproteolysis of a monomeric precursor within a distinctive protein motif called sea urchin-enterokinase-agrin (SEA) domain, yet the purpose of this cleavage and heterodimer creation is uncertain. In this study, we identify a functional nuclear localization signal within beta-DG and show that, in addition to associating with alpha-DG at the cell surface, the full-length and glycosylated beta-DG autonomously traffics to the cytoplasm and nucleoplasm in a process that occurs independent of alpha-DG ligand binding. The trafficking pattern of beta-DG mirrors that of MUC1-C, the transmembrane subunit of the related MUC1 oncoprotein, also a heterodimeric membrane-tethered mucin created by SEA autoproteolysis. We show that the transmembrane subunits of both MUC1 and DG transit the secretory pathway prior to nuclear targeting and that their monomeric precursors maintain the capacity for nuclear trafficking. A screen of breast carcinoma cell lines of distinct pathophysiological origins revealed considerable variability in the nuclear partitioning of beta-DG, indicating that nuclear localization of beta-DG is regulated, albeit independent of extracellular ligand binding. These findings point to novel intracellular functions for beta-DG, with possible disease implications. They also reveal an evolutionarily conserved role for SEA autoproteolysis, serving to enable independent functions of mucin transmembrane subunits, enacted by a shared and poorly understood pathway of segregated subunit trafficking.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceAnimalsCarcinomaCell Line, TumorCell NucleusCytoplasmDystroglycansHumansMolecular Sequence DataMucinsSequence AlignmentDystroglycansMucins

Identifiers

PMID18764929
PMCPMC2950207
OpenAlexW2068012012

What OpenQuestion holds

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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.