Evidence map›Paper›PMID 19361519›Full record

ArticleJournal of molecular biology2009

Kinetic analysis of the guanine nucleotide exchange activity of TRAPP, a multimeric Ypt1p exchange factor.

Harvey F Chin, Yiying Cai, Shekar Menon, Susan Ferro-Novick, Karin M Reinisch, Enrique M De La Cruz

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. 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
1.7field-weighted citation impact, top 18% 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, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Rab GTPase regulation of membrane identity.Current opinion in cell biology · 2013
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Rab GEFs and GAPs.Current opinion in cell biology · 2010
    Review
  20. 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

6 authors at 3 institutions in 1 country.

Harvey F ChinDepartment of Molecular Biophysics and Biochemistry, Yale University, PO Box 208114, 260 Whitney Avenue, New Haven, CT 06520-8114, USA.
Yiying Cai
Shekar Menon
Susan Ferro-Novick
Karin M Reinisch
Enrique M De La Cruz
Yale University · USHoward Hughes Medical Institute · USWhitney Museum of American Art · US

Funding

Regulatory Mechanisms in Membrane TraffickingR01GM080616 · NIGMS · YALE UNIVERSITY · PI REINISCH, KARIN M · 2007 to 2018
$4.1M
Functional diversity of myosin VIIR01GM071688 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2007 to 2010
$1.2M
Defining Effects of Myosin VII Structure and Kinetics on Hereditary DeafnessF31DC009143 · NIDCD · YALE UNIVERSITY · PI CHIN, HARVEY F. · 2007 to 2008
$82k
Howard Hughes Medical InstituteNIDCD NIH HHS F31 DC009143NIDCD NIH HHS F31 DC009143-01NIGMS NIH HHS GM071688NIGMS NIH HHS GM080616NIGMS NIH HHS R01 GM071688NIGMS NIH HHS R01 GM080616
6 · The paper itself

Abstract

TRAPP complexes, which are large multimeric assemblies that function in membrane traffic, are guanine nucleotide exchange factors (GEFs) that activate the Rab GTPase Ypt1p. Here we measured rate and equilibrium constants that define the interaction of Ypt1p with guanine nucleotide (guanosine 5'-diphosphate and guanosine 5'-triphosphate/guanosine 5'-(beta,gamma-imido)triphosphate) and the core TRAPP subunits required for GEF activity. These parameters allowed us to identify the kinetic and thermodynamic bases by which TRAPP catalyzes nucleotide exchange from Ypt1p. Nucleotide dissociation from Ypt1p is slow (approximately 10(-4) s(-1)) and accelerated >1000-fold by TRAPP. Acceleration of nucleotide exchange by TRAPP occurs via a predominantly Mg(2+)-independent pathway. Thermodynamic linkage analysis indicates that TRAPP weakens nucleotide affinity by <80-fold and vice versa, in contrast to most other characterized GEF systems that weaken nucleotide binding affinities by 4-6 orders of magnitude. The overall net changes in nucleotide binding affinities are small because TRAPP accelerates both nucleotide binding and dissociation from Ypt1p. Weak thermodynamic coupling allows TRAPP, Ypt1p, and nucleotide to exist as a stable ternary complex, analogous to strain-sensing cytoskeleton motors. These results illustrate a novel strategy of guanine nucleotide exchange by TRAPP that is particularly suited for a multifunctional GEF involved in membrane traffic.

Indexed as

Escherichia coliGuanine Nucleotide Exchange FactorsGuanine NucleotidesKineticsProtein BindingProtein Subunitsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsThermodynamicsTransduction, GeneticVesicular Transport ProteinsGuanine Nucleotide Exchange FactorsGuanine NucleotidesProtein Subunitsrab GTP-Binding ProteinsSaccharomyces cerevisiae Proteinstransport protein particle, TRAPPVesicular Transport ProteinsYPT1 protein, S cerevisiae

Identifiers

PMID19361519
PMCPMC2770256
OpenAlexW1967921550

What OpenQuestion holds

Textmetadata
LicenceTDM
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.