Evidence map›Paper›PMID 30726745›Full record

ArticleCell reports2019

Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.

Ye Dee Tay, Marcin Leda, Christos Spanos, Juri Rappsilber, Andrew B Goryachev, Kenneth E Sawin

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

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  9. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
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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 2 institutions in 2 countries.

Ye Dee TayWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK.
Marcin LedaSynthSys-Centre for Synthetic and Systems Biology, School of Biological Sciences, University of Edinburgh, CH Waddington Building, Max Born Crescent, Edinburgh EH9 3BF, UK.
Christos SpanosWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK.
Juri RappsilberWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK; Chair of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, 13355, Germany.
Andrew B GoryachevSynthSys-Centre for Synthetic and Systems Biology, School of Biological Sciences, University of Edinburgh, CH Waddington Building, Max Born Crescent, Edinburgh EH9 3BF, UK. Electronic address: andrew.goryachev@ed.ac.uk.
Kenneth E SawinWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK. Electronic address: ken.sawin@ed.ac.uk.
Wellcome Centre for Cell Biology · GBUniversity of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K021699/1Wellcome Trust 091020Wellcome Trust 094517Wellcome Trust 101527Wellcome Trust 103139/Z/13/ZWellcome Trust 108504Wellcome Trust 203149Wellcome Trust 210659Wellcome Trust 210659/Z/18/Z
6 · The paper itself

Abstract

NDR/LATS kinases regulate multiple aspects of cell polarity and morphogenesis from yeast to mammals. Fission yeast NDR/LATS kinase Orb6 has been proposed to control cell polarity by regulating the Cdc42 guanine nucleotide exchange factor Gef1. Here, we show that Orb6 regulates polarity largely independently of Gef1 and that Orb6 positively regulates exocytosis. Through Orb6 inhibition in vivo and quantitative global phosphoproteomics, we identify Orb6 targets, including proteins involved in membrane trafficking. We confirm Sec3 and Sec5, conserved components of the exocyst complex, as substrates of Orb6 both in vivo and in vitro, and we show that Orb6 kinase activity is important for exocyst localization to cell tips and for exocyst activity during septum dissolution after cytokinesis. We further find that Orb6 phosphorylation of Sec3 contributes to exocyst function in concert with exocyst protein Exo70. We propose that Orb6 contributes to polarized growth by regulating membrane trafficking at multiple levels.

Indexed as

Gene Expression Regulation, FungalCell Cycle ProteinsCell PolarityCytokinesisExocytosisPhosphoproteinsPhosphorylationProtein IsoformsProtein Serine-Threonine KinasesProteomicsRho Guanine Nucleotide Exchange FactorsSaccharomyces cerevisiaeSchizosaccharomycesSchizosaccharomyces pombe ProteinsVesicular Transport ProteinsCell Cycle ProteinsEXO70 protein, S pombeGef1 protein, S pombeOrb6 protein, S pombePhosphoproteinsProtein IsoformsProtein Serine-Threonine KinasesRho Guanine Nucleotide Exchange FactorsSchizosaccharomyces pombe ProteinsSec3 protein, S pombeVesicular Transport ProteinsCdc42exocystexocytosisfission yeastNDR/LATS kinaseOrb6phosphoproteomicsphosphorylationSchizosaccharomyces pombeSec3

Identifiers

PMID30726745
PMCPMC6367570
OpenAlexW2949787467

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.