Evidence map›Paper›PMID 10760272›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16.

B Zheng, D Chen, M G Farquhar

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. GDPD5 is a glycerophosphocholine phosphodiesterase that osmotically regulates the osmoprotective organic osmolyte GPC.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  20. 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

3 authors at 1 institution in 1 country.

B ZhengDepartment of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0651, USA.
D Chen
M G Farquhar
University of California, San Diego · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI FARQUHAR, MARILYN GIST · 1993 to 2002
$5.0M
SECRETION AND GOLGI TRAFFIC IN PITUITARY AND OTHER CELLSR01DK017780 · NIDDK · YALE UNIVERSITY · PI FARQUHAR, MARILYN GIST · 1986 to 2010
$3.7M
SECRETION AND GOLGI TRAFFIC IN PITUITARY AND OTHER CELLSR37DK017780 · NIDDK · YALE UNIVERSITY · PI FARQUHAR, MARILYN GIST · 1988 to 1995
–
NCI NIH HHS CA58689NIDDK NIH HHS DK17780NIDDK NIH HHS R01 DK017780
6 · The paper itself

Abstract

We have identified the protein MIR16 (for Membrane Interacting protein of RGS16) from a yeast two-hybrid screen by using RGS16 as bait. MIR16 shares strong homology with bacterial glycerophosphodiester phosphodiesterases. It interacts with RGS16 and, more weakly, with several other selected RGS proteins. Analysis of deletion mutants showed that the N-terminal region of the RGS domain in RGS16 is required for its interaction with MIR16. MIR16 is an integral membrane glycoprotein, because it remained associated with membrane fractions after alkaline treatment and because, in some cells, it is sensitive to digestion with endoglycosidase H. By immunofluorescence and immunoelectron microscopy, MIR16 was localized on the plasma membrane in liver and kidney and on intracellular membranes in rat pituitary and cultured pituitary cells. MIR16 represents the only integral membrane protein identified thus far to interact with an RGS domain and, to our knowledge, is the only mammalian glycerophosphodiester phosphodiesterase that has been cloned. The putative enzymatic activity of MIR16 and its interaction with RGS16 suggest that it may play important roles in lipid metabolism and in G protein signaling.

Indexed as

Amino Acid SequenceAnimalsCell LineCloning, MolecularDNA, ComplementaryHumansMembrane ProteinsMolecular Sequence DataPhosphoric Diester HydrolasesProtein BindingRatsRGS ProteinsRNA, MessengerSequence Homology, Amino AcidSubcellular FractionsDNA, Complementaryglycerophosphodiester phosphodiesteraseMembrane ProteinsPhosphoric Diester HydrolasesRGS ProteinsRNA, Messenger

Identifiers

PMID10760272
PMCPMC18131
OpenAlexW1983362881

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.