Evidence map›Paper›PMID 14657246›Full record

ArticleMolecular biology of the cell2004

The EF-hand Ca2+-binding protein p22 plays a role in microtubule and endoplasmic reticulum organization and dynamics with distinct Ca2+-binding requirements.

Josefa Andrade, Hu Zhao, Brian Titus, Sandra Timm Pearce, Margarida Barroso

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. ER structure and function.Current opinion in cell biology · 2013
    Review
  6. Calcineurin homologous protein: a multifunctional Ca2+-binding protein family.American journal of physiology. Renal physiology · 2012
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Roles and origins of leukocyte lipid bodies: proteomic and ultrastructural studies.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2007
    Article
  20. Endoplasmic reticulum architecture: structures in flux.Current opinion in cell biology · 2006
    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 1 institution in 1 country.

Josefa AndradeAlbany Medical Center; Center for Cardiovascular Sciences, Albany, New York 12208, USA.
Hu Zhao
Brian Titus
Sandra Timm Pearce
Margarida Barroso
Albany Medical Center Hospital · US

Funding

REGULATION OF CYTOSKELETON AND MEMBRANE TRAFFIC BY P22R01GM057519 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BARROSO, MARGARIDA · 1998 to 2002
$549k
NIGMS NIH HHS R01 GM057519NIGMS NIH HHS R01-GM57519
6 · The paper itself

Abstract

We have reported that p22, an N-myristoylated EF-hand Ca(2+)-binding protein, associates with microtubules and plays a role in membrane trafficking. Here, we show that p22 also associates with membranes of the early secretory pathway membranes, in particular endoplasmic reticulum (ER). On binding of Ca(2+), p22's ability to associate with membranes increases in an N-myristoylation-dependent manner, which is suggestive of a nonclassical Ca(2+)-myristoyl switch mechanism. To address the intracellular functions of p22, a digitonin-based "bulk microinjection" assay was developed to load cells with anti-p22, wild-type, or mutant p22 proteins. Antibodies against a p22 peptide induce microtubule depolymerization and ER fragmentation; this antibody-mediated effect is overcome by preincubation with the respective p22 peptide. In contrast, N-myristoylated p22 induces the formation of microtubule bundles, the accumulation of ER structures along the bundles as well as an increase in ER network formation. An N-myristoylated Ca(2+)-binding p22 mutant, which is unable to undergo Ca(2+)-mediated conformational changes, induces microtubule bundling and accumulation of ER structures along the bundles but does not increase ER network formation. Together, these data strongly suggest that p22 modulates the organization and dynamics of microtubule cytoskeleton in a Ca(2+)-independent manner and affects ER network assembly in a Ca(2+)-dependent manner.

Indexed as

EF Hand MotifsAnimalsCalcium-Binding ProteinsCytoplasmic VesiclesEndoplasmic ReticulumIntracellular MembranesLipoproteinsLiverMicroscopy, ConfocalMicrotubulesRatsRats, Sprague-DawleyRecombinant Proteinscalcium binding protein p22, ratCalcium-Binding ProteinsLipoproteinsRecombinant Proteins

Identifiers

PMID14657246
PMCPMC329218
OpenAlexW2165922880

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.