Evidence map›Paper›PMID 20032513›Full record

ArticleAmerican journal of physiology. Cell physiology2010

Tumor protein D52 expression and Ca2+-dependent phosphorylation modulates lysosomal membrane protein trafficking to the plasma membrane.

Diana D H Thomas, Christina L Martin, Ning Weng, Jennifer A Byrne, Guy E Groblewski

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Tumor protein D52 (TPD52) and cancer-oncogene understudy or understudied oncogene?Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Review
  12. Article
  13. Tumor protein D52 controls trafficking of an apical endolysosomal secretory pathway in pancreatic acinar cells.American journal of physiology. Gastrointestinal and liver physiology · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Regulation of acinar cell function in the pancreas.Current opinion in gastroenterology · 2010
    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 2 countries.

Diana D H ThomasUniv. of Wisconsin, Dept. of Nutritional Sciences, 1415 Linden Dr., Madison, WI 53706, USA.
Christina L Martin
Ning Weng
Jennifer A Byrne
Guy E Groblewski
University of Wisconsin–Madison · USChildren's Hospital at Westmead · AU

Funding

NIDDK NIH HHS DK07088
6 · The paper itself

Abstract

Tumor protein D52 (also known as CRHSP-28) is highly expressed in multiple cancers and tumor-derived cell lines; however, it is normally abundant in secretory epithelia throughout the digestive system, where it has been implicated in Ca(2+)-dependent digestive enzyme secretion (41). Here we demonstrate, using site-specific mutations, that Ca(2+)-sensitive phosphorylation at serine 136 modulates the accumulation of D52 at the plasma membrane within 2 min of cell stimulation. When expressed in Chinese hamster ovary CHO-K1 cells, D52 colocalized with adaptor protein AP-3, Rab27A, vesicle-associated membrane protein VAMP7, and lysosomal-associated membrane protein LAMP1, all of which are present in lysosome-like secretory organelles. Overexpression of D52 resulted in a marked accumulation of LAMP1 on the plasma membrane that was further enhanced following elevation of cellular Ca(2+). Strikingly, mutation of serine 136 to alanine abolished the Ca(2+)-stimulated accumulation of LAMP1 at the plasma membrane whereas phosphomimetic mutants constitutively induced LAMP1 plasma membrane accumulation independent of elevated Ca(2+). Identical results were obtained for endogenous D52 in normal rat kidney and HeLA cells, where both LAMP1 and D52 rapidly accumulated on the plasma membrane in response to elevated cellular Ca(2+). Finally, D52 induced the uptake of LAMP1 antibodies from the cell surface in accordance with both the level of D52 expression and phosphorylation at serine 136 demonstrating that D52 altered the plasma membrane recycling of LAMP1-associated secretory vesicles. These findings implicate both D52 expression and Ca(2+)-dependent phosphorylation at serine 136 in lysosomal membrane trafficking to and from the plasma membrane providing a novel Ca(2+)-sensitive pathway modulating the lysosome-like secretory pathway.

Indexed as

Adaptor Protein Complex 3Amino Acid SequenceAnimalsCalciumCell MembraneCHO CellsCricetinaeCricetulusFluorescent Antibody TechniqueHeLa CellsHumansLysosomal-Associated Membrane Protein 1LysosomesMicroscopy, FluorescenceMolecular Sequence DataMutagenesis, Site-DirectedAdaptor Protein Complex 3CalciumLysosomal-Associated Membrane Protein 1Neoplasm Proteinsrab GTP-Binding ProteinsR-SNARE ProteinsSerineTPD52 protein, human

Identifiers

PMID20032513
PMCPMC2838566
OpenAlexW2089681519

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.