Evidence map›Paper›PMID 15563607›Full record

ArticleMolecular biology of the cell2005

The yeast par-1 homologs kin1 and kin2 show genetic and physical interactions with components of the exocytic machinery.

Maya Elbert, Guendalina Rossi, Patrick Brennwald

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.6field-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

46 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Phosphoinositides and Membrane Targeting in Cell Polarity.Cold Spring Harbor perspectives in biology · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Regulation of Cell Polarity by PAR-1/MARK Kinase.Current topics in developmental biology · 2017
    Review
  16. Review
  17. The Kinome of Edible and Medicinal FungusFrontiers in microbiology · 2016
    Article
  18. Article
  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 2 institutions in 1 country.

Maya ElbertDepartment of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Guendalina Rossi
Patrick Brennwald
University of North Carolina at Chapel Hill · USCornell University · US

Funding

REGULATION OF EXOCYTOSIS BY A RHO GTPPASER01GM054712 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI PATRICK J BRENNWALD · 1998 to 2026
$9.5M
TRI-INSTITUTIONAL TRAINING PROGRAM IN VISION RESEARCHT32EY007138 · NEI · WEILL MEDICAL COLL OF CORNELL UNIV · PI RODRIGUEZ-BOULAN, ENRIQUE J · 1994 to 2013
$3.2M
NEI NIH HHS T32 EY007138NEI NIH HHS T32EY007138NIGMS NIH HHS GM-54712NIGMS NIH HHS R01 GM054712
6 · The paper itself

Abstract

Kin1 and Kin2 are Saccharomyces cerevisiae counterparts of Par-1, the Caenorhabditis elegans kinase essential for the establishment of polarity in the one cell embryo. Here, we present evidence for a novel link between Kin1, Kin2, and the secretory machinery of the budding yeast. We isolated KIN1 and KIN2 as suppressors of a mutant form of Rho3, a Rho-GTPase acting in polarized trafficking. Genetic analysis suggests that KIN1 and KIN2 act downstream of the Rab-GTPase Sec4, its exchange factor Sec2, and several components of the vesicle tethering complex, the Exocyst. We show that Kin1 and Kin2 physically interact with the t-SNARE Sec9 and the Lgl homologue Sro7, proteins acting at the final stage of exocytosis. Structural analysis of Kin2 reveals that its catalytic activity is essential for its function in the secretory pathway and implicates the conserved 42-amino acid tail at the carboxy terminal of the kinase in autoinhibition. Finally, we find that Kin1 and Kin2 induce phosphorylation of t-SNARE Sec9 in vivo and stimulate its release from the plasma membrane. In summary, we report the finding that yeast Par-1 counterparts are associated with and regulate the function of the exocytic apparatus via phosphorylation of Sec9.

Indexed as

ExocytosisAmino Acid SequenceAmino Acid SubstitutionCatalytic DomainCell FractionationConserved SequenceFungal ProteinsGlutathione TransferaseMembrane ProteinsMethionineMolecular Sequence DataPhosphoproteinsPoint MutationPrecipitin TestsProtein BindingProtein Serine-Threonine KinasesFungal ProteinsGlutathione TransferaseKIN1 protein, S cerevisiaeKIN2 protein, S cerevisiaeMembrane ProteinsMethioninePhosphoproteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID15563607
PMCPMC545889
OpenAlexW2160532938

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.