Evidence map›Paper›PMID 18843045›Full record

ArticleMolecular biology of the cell2008

The yeast LATS/Ndr kinase Cbk1 regulates growth via Golgi-dependent glycosylation and secretion.

Cornelia Kurischko, Venkata K Kuravi, Nattha Wannissorn, Pavel A Nazarov, Michelle Husain, Chao Zhang, Kevan M Shokat, J Michael McCaffery, Francis C Luca

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-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

22 citing papers in PubMed, 43 citations in OpenAlex.

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  11. Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners.Proceedings of the National Academy of Sciences of the United States of America · 2013
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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

9 authors at 3 institutions in 1 country.

Cornelia KurischkoDepartment of Animal Biology and the Mari Lowe Center for Comparative Oncology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Venkata K Kuravi
Nattha Wannissorn
Pavel A Nazarov
Michelle Husain
Chao Zhang
Kevan M Shokat
J Michael McCaffery
Francis C Luca
University of Pennsylvania · USHoward Hughes Medical Institute · USJohns Hopkins University · US

Funding

Characterization of the Mitotic Exit NetworkR01GM060575 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LUCA, FRANCIS C · 2000 to 2010
$2.7M
SPECIFIC INHIBITOR OF LCK TO PROBE T CELL SIGNALINGR01AI044009 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SHOKAT, KEVAN M. · 1998 to 2006
$2.1M
NIAID NIH HHS AI44009NIAID NIH HHS R01 AI044009NIGMS NIH HHS GM-60575NIGMS NIH HHS R01 GM060575
6 · The paper itself

Abstract

Saccharomyces cerevisiae Cbk1 is a LATS/Ndr protein kinase and a downstream component of the regulation of Ace2 and morphogenesis (RAM) signaling network. Cbk1 and the RAM network are required for cellular morphogenesis, cell separation, and maintenance of cell integrity. Here, we examine the phenotypes of conditional cbk1 mutants to determine the essential function of Cbk1. Cbk1 inhibition severely disrupts growth and protein secretion, and triggers the Swe1-dependent morphogenesis checkpoint. Cbk1 inhibition also delays the polarity establishment of the exocytosis regulators Rab-GTPase Sec4 and its exchange factor Sec2, but it does not interfere with actin polarity establishment. Cbk1 binds to and phosphorylates Sec2, suggesting that it regulates Sec4-dependent exocytosis. Intriguingly, Cbk1 inhibition causes a >30% decrease in post-Golgi vesicle accumulation in late secretion mutants, indicating that Cbk1 also functions upstream of Sec2-Sec4, perhaps at the level of the Golgi. In agreement, conditional cbk1 mutants mislocalize the cis-Golgi mannosyltransferase Och1, are hypersensitive to the aminoglycoside hygromycin B, and exhibit diminished invertase and Sim1 glycosylation. Significantly, the conditional lethality and hygromycin B sensitivity of cbk1 mutants are suppressed by moderate overexpression of several Golgi mannosyltransferases. These data suggest that an important function for Cbk1 and the RAM signaling network is to regulate growth and secretion via Golgi and Sec2/Sec4-dependent processes.

Indexed as

Saccharomyces cerevisiaeAnthelminticsCell CycleCell Cycle ProteinsCell PolarityCytoskeletonFluorescent DyesFungal ProteinsGlucan Endo-1,3-beta-D-GlucosidaseGlycosylationGolgi ApparatusGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsHygromycin BIntracellular Signaling Peptides and ProteinsMannosyltransferasesAnthelminticsBGL2 protein, S cerevisiaeCBK1 protein, S cerevisiaeCell Cycle ProteinsFluorescent DyesFM 4-64Fungal ProteinsGlucan Endo-1,3-beta-D-GlucosidaseGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsHygromycin BIntracellular Signaling Peptides and ProteinsMannosyltransferasesMembrane GlycoproteinsOCH1 protein, S cerevisiaeProtein Serine-Threonine KinasesProtein-Tyrosine KinasesPyridinium CompoundsQuaternary Ammonium Compoundsrab GTP-Binding ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSEC2 protein, S cerevisiaeSEC4 protein, S cerevisiaeSWE1 protein, S cerevisiae

Identifiers

PMID18843045
PMCPMC2592669
OpenAlexW2166044740

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.