Evidence map›Paper›PMID 23091056›Full record

ArticleThe Journal of biological chemistry2012

Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase.

Ganesh V Pusapati, Giovanni Luchetti, Suzanne R Pfeffer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

48 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Review
  9. EMT activates exocytotic Rabs to coordinate invasion and immunosuppression in lung cancer.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. AFrontiers in genetics · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Arf1 orchestrates Rab GTPase conversion at theMolecular biology of the cell · 2021
    Article
  17. Article
  18. Review
  19. 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.

Ganesh V PusapatiDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
Giovanni Luchetti
Suzanne R Pfeffer
Stanford University · US

Funding

INTRACELLULAR TRANSPORT--THE MANNOSE/PHOSPHATE RECEPTORR01DK037332 · NIDDK · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 1986 to 2019
$4.7M
INTRACELLULAR TRANSPORT--THE MANNOSE-PHOSPHATE RECEPTORR37DK037332 · NIDDK · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 1999 to 2008
$3.4M
Intracellular Transport-The Mannose Phosphate ReceptorR56DK037332 · NIDDK · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 2014 to 2014
$120k
NIDDK NIH HHS DK37332NIDDK NIH HHS R01 DK037332NIDDK NIH HHS R37 DK037332NIDDK NIH HHS R56 DK037332NIGMS NIH HHS GM007276
6 · The paper itself

Abstract

Rab GTPases are master regulators of membrane trafficking events and template the directionality of protein transport through the secretory and endocytic pathways. Certain Rabs recruit the guanine nucleotide exchange factor (GEF) that activates a subsequent acting Rab protein in a given pathway; this process has been termed a Rab cascade. We show here that the medial Golgi-localized Rab33B GTPase has the potential to link functionally to the late Golgi, Rab6 GTPase, by its capacity for association with Ric1 and Rgp1 proteins. In yeast, Ric1p and Rgp1p form a complex that catalyzes guanine nucleotide exchange by Ypt6p, the Rab6 homolog. Human Ric1 and Rgp1 both bind Rab6A with preference for the GDP-bound conformation, characteristic of a GEF. Nevertheless, both Ric1 and Rgp1 proteins are needed to catalyze nucleotide exchange on Rab6A protein. Ric1 and Rgp1 form a complex, but unlike their yeast counterparts, most of the subunits are not associated, and most of the proteins are cytosolic. Loss of Ric1 or Rgp1 leads to destabilization of Rab6, concomitant with a block in Rab6-dependent retrograde transport of mannose 6-phosphate receptors to the Golgi. The C terminus of Ric1 protein contains a distinct binding site for Rab33B-GTP, supporting the existence of a Rab cascade between the medial and trans Golgi. This study thus identifies a GEF for Rab6A in human cells.

Indexed as

Endoplasmic ReticulumEnzyme StabilityGuanine Nucleotide Exchange FactorsHeLa CellsHumansMembrane ProteinsMultiprotein ComplexesProtein BindingProtein Structure, Tertiaryrab GTP-Binding Proteinstrans-Golgi NetworkGuanine Nucleotide Exchange FactorsMembrane ProteinsMultiprotein ComplexesRAB33B protein, humanRab6 proteinrab GTP-Binding Proteins

Identifiers

PMID23091056
PMCPMC3516758
OpenAlexW1985842539

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.