Evidence map›Paper›PMID 16822837›Full record

ArticleMolecular biology of the cell2006

The STE20/germinal center kinase POD6 interacts with the NDR kinase COT1 and is involved in polar tip extension in Neurospora crassa.

Stephan Seiler, Nico Vogt, Carmit Ziv, Rena Gorovits, Oded Yarden

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed, 66 citations in OpenAlex.

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  6. RNAi-Mediated Gene Silencing ofJournal of microbiology and biotechnology · 2020
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  13. TheFrontiers in microbiology · 2017
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  18. STRIPAK complexes: structure, biological function, and involvement in human diseases.The international journal of biochemistry & cell biology · 2014
    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

5 authors at 2 institutions in 2 countries.

Stephan SeilerDeutsche Forschungsgemeinschaft Research Center of Molecular Physiology of the Brain (CMPB), Abteilung Molekulare Mikrobiologie, Universität Göttingen, D-37077 Göttingen, Germany. sseiler@gwdg.de
Nico Vogt
Carmit Ziv
Rena Gorovits
Oded Yarden
Hebrew University of Jerusalem · ILUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the Ste20 and NDR protein kinase families are important for normal cell differentiation and morphogenesis in various organisms. We characterized POD6 (NCU02537.2), a novel member of the GCK family of Ste20 kinases that is essential for hyphal tip extension and coordinated branch formation in the filamentous fungus Neurospora crassa. pod-6 and the NDR kinase mutant cot-1 exhibit indistinguishable growth defects, characterized by cessation of cell elongation, hyperbranching, and altered cell-wall composition. We suggest that POD6 and COT1 act in the same genetic pathway, based on the fact that both pod-6 and cot-1 can be suppressed by 1) environmental stresses, 2) altering protein kinase A activity, and 3) common extragenic suppressors (ropy, as well as gul-1, which is characterized here as the ortholog of the budding and fission yeasts SSD1 and Sts5, respectively). Unlinked noncomplementation of cot-1/pod-6 alleles indicates a potential physical interaction between the two kinases, which is further supported by coimmunoprecipitation analyses, partial colocalization of both proteins in wild-type cells, and their common mislocalization in dynein/kinesin mutants. We conclude that POD6 acts together with COT1 and is essential for polar cell extension in a kinesin/dynein-dependent manner in N. crassa.

Indexed as

Cell PolarityAmino Acid SequenceCatalytic DomainCyclic AMP-Dependent Protein KinasesFungal ProteinsGerminal Center KinasesHyphaeMicrotubulesMolecular Motor ProteinsMolecular Sequence DataMutationNeurospora crassaPhenotypeProtein BindingProtein Serine-Threonine KinasesProtein TransportCyclic AMP-Dependent Protein KinasesFungal ProteinsGerminal Center KinasesMolecular Motor ProteinsProtein Serine-Threonine KinasesSodium Chloride

Identifiers

PMID16822837
PMCPMC1593175
OpenAlexW2131372853

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.