Evidence map›Paper›PMID 27760305›Full record

ArticleJournal of molecular biology2016

Differences in the Phosphorylation-Dependent Regulation of Prenylation of Rap1A and Rap1B.

Jessica M Wilson, Jeremy W Prokop, Ellen Lorimer, Elizabeth Ntantie, Carol L Williams

Abstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Trial
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  11. Integration of Rap1 and Calcium Signaling.International journal of molecular sciences · 2020
    Review
  12. Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. The Many Faces of Rap1 GTPase.International journal of molecular sciences · 2018
    Review
  17. GEF mechanism revealed by the structure of SmgGDS-558 and farnesylated RhoA complex and its implication for a chaperone mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. 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

5 authors at 3 institutions in 1 country.

Jessica M WilsonDepartment of Pharmacology and Toxicology, Cancer Center and Cardiovascular Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Jeremy W ProkopHudsonAlpha Institute for Biotechnology, 601 Genome Way NW, Huntsville, AL 35806, USA.
Ellen LorimerDepartment of Pharmacology and Toxicology, Cancer Center and Cardiovascular Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Elizabeth NtantieCollege of Pharmacy and Pharmaceutical Sciences, Florida A&M University, 1415 South Martin Luther King Jr. Boulevard, Tallahassee, FL 32307, USA.
Carol L WilliamsDepartment of Pharmacology and Toxicology, Cancer Center and Cardiovascular Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA. Electronic address: williams@mcw.edu.
Medical College of Wisconsin · USFlorida Agricultural and Mechanical University · USHudsonAlpha Institute for Biotechnology · US

Funding

Medical Scientist Training ProgramT32GM080202 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI BARBIERI, JOSEPH T, SALZMAN, NITA H · 2010 to 2024
$5.7M
Regulation of Rap1 Prenylation and Trafficking in Breast CancerR01CA188871 · NCI · MEDICAL COLLEGE OF WISCONSIN · PI WILLIAMS, CAROL LUCILLE · 2015 to 2019
$1.7M
Using a Sequence-to-Structure-to-Function Approach to Functionally Characterize Protein Coding Missense Mutations in the Human and Rat GenomesK01ES025435 · NIEHS · MICHIGAN STATE UNIVERSITY · PI PROKOP, JEREMY WILLIAM · 2014 to 2018
$489k
NCI NIH HHS R01 CA188871NIEHS NIH HHS K01 ES025435NIGMS NIH HHS T32 GM080202
6 · The paper itself

Abstract

Two isoforms of the small GTPase Rap1, Rap1A and Rap1B, participate in cell adhesion; Rap1A promotes steady state adhesion, while Rap1B regulates dynamic changes in cell adhesion. These events depend on the prenylation of Rap1, which promotes its membrane localization. Here, we identify previously unsuspected differences in the regulation of prenylation of Rap1A versus Rap1B, due in part to their different phosphorylation-dependent interactions with the chaperone protein SmgGDS-607. Previous studies indicate that the activation of Gα

Indexed as

PrenylationProtein Processing, Post-TranslationalAmino Acid SequenceCell LineGuanine Nucleotide Exchange FactorsHumansModels, MolecularMolecular Sequence DataPhosphorylationProtein BindingProtein ConformationProtein Interaction Mappingrap1 GTP-Binding Proteinsrap GTP-Binding ProteinsSequence AlignmentGuanine Nucleotide Exchange FactorsRAP1A protein, humanRAP1B protein, humanRAP1GDS1 protein, humanrap1 GTP-Binding Proteinsrap GTP-Binding ProteinsG protein-coupled receptorpolybasic regionprotein isoprenylationRap1GDS1SmgGDS

Identifiers

PMID27760305
PMCPMC5153279
OpenAlexW2536106356

What OpenQuestion holds

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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.