Evidence map›Paper›PMID 8986788›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.

L De Vries, E Elenko, L Hubler, T L Jones, M G Farquhar

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

51 citing papers in PubMed, 165 citations in OpenAlex.

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  9. High-resolution structure of RGS17 suggests a role for CaThe Journal of biological chemistry · 2019
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  20. A finer tuning of G-protein signaling through regulated control of RGS proteins.American journal of physiology. Heart and circulatory physiology · 2012
    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.

L De VriesDivision of Cellular and Molecular Medicine, University of California at San Diego, La Jolla 92093-0651, USA.
E Elenko
L Hubler
T L Jones
M G Farquhar
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI GILL, GORDON N · 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
GLYCOSYLATION AND GOLDI TRAFFIC IN VITROF32CA066289 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI HUBLER, LAURA · 1995 to 1997
–
SECRETION AND GOLGI TRAFFIC IN PITUITARY AND OTHER CELLSR37DK017780 · NIDDK · YALE UNIVERSITY · PI FARQUHAR, MARILYN GIST · 1988 to 1995
–
NCI NIH HHS CA58689NCI NIH HHS F32 CA066289NIDDK NIH HHS DK17780NIDDK NIH HHS R01 DK017780NIGMS NIH HHS GM07752NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

GAIP (G Alpha Interacting Protein) is a member of the recently described RGS (Regulators of G-protein Signaling) family that was isolated by interaction cloning with the heterotrimeric G-protein G alpha i3 and was recently shown to be a GTPase-activating protein (GAP). In AtT-20 cells stably expressing GAIP, we found that GAIP is membrane-anchored and faces the cytoplasm, because it was not released by sodium carbonate treatment but was digested by proteinase K. When Cos cells were transiently transfected with GAIP and metabolically labeled with [35S]methionine, two pools of GAIP--a soluble and a membrane-anchored pool--were found. Since the N terminus of GAIP contains a cysteine string motif and cysteine string proteins are heavily palmitoylated, we investigated the possibility that membrane-anchored GAIP might be palmitoylated. We found that after labeling with [3H]palmitic acid, the membrane-anchored pool but not the soluble pool was palmitoylated. In the yeast two-hybrid system, GAIP was found to interact specifically with members of the G alpha i subfamily, G alpha i1, G alpha i2, G alpha i3, G alpha z, and G alpha o, but not with members of other G alpha subfamilies, G alpha s, G alpha q, and G alpha 12/13. The C terminus of G alpha i3 is important for binding because a 10-aa C-terminal truncation and a point mutant of G alpha i3 showed significantly diminished interaction. GAIP interacted preferentially with the activated (GTP) form of G alpha i3, which is in keeping with its GAP activity. We conclude that GAIP is a membrane-anchored GAP with a cysteine string motif. This motif, present in cysteine string proteins found on synaptic vesicles, pancreatic zymogen granules, and chromaffin granules, suggests GAIP's possible involvement in membrane trafficking.

Indexed as

Amino Acid SequenceAnimalsCattleCell MembraneCloning, MolecularCOS CellsGTP-Binding ProteinsHumansMacromolecular SubstancesMiceMolecular Sequence DataPalmitic AcidPhosphoproteinsPolymerase Chain ReactionProtein Processing, Post-TranslationalRatsGTP-Binding ProteinsMacromolecular SubstancesPalmitic AcidPhosphoproteinsRecombinant Proteinsregulator of G-protein signalling 19RGS Proteins

Identifiers

PMID8986788
PMCPMC26381
OpenAlexW2170755436

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.