Evidence map›Paper›PMID 12181352›Full record

ArticleMolecular biology of the cell2002

The MEK kinase Ssk2p promotes actin cytoskeleton recovery after osmotic stress.

Tatiana Yuzyuk, Marissa Foehr, David C Amberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

32 citing papers in PubMed, 52 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Tatiana YuzyukDepartment of Biochemistry and Molecular Biology, State University of New York (SUNY) Upstate Medical University, Syracuse 13210, USA.
Marissa Foehr
David C Amberg
SUNY Upstate Medical University · USWadsworth Center · US

Funding

Regulation of Actin DynamicsR01GM056189 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI AMBERG, DAVID C · 1998 to 2010
$2.3M
NIGMS NIH HHS GM56189NIGMS NIH HHS R01 GM056189
6 · The paper itself

Abstract

Saccharomyces cerevisiae adapts to osmotic stress through the activation of a conserved high-osmolarity growth (HOG) mitogen-activated protein (MAP) kinase pathway. Transmission through the HOG pathway is very well understood, yet other aspects of the cellular response to osmotic stress remain poorly understood, most notably regulation of actin organization. The actin cytoskeleton rapidly disassembles in response to osmotic insult and is induced to reassemble only after osmotic balance with the environment is reestablished. Here, we show that one of three MEK kinases of the HOG pathway, Ssk2p, is specialized to facilitate actin cytoskeleton reassembly after osmotic stress. Within minutes of cells' experiencing osmotic stress or catastrophic disassembly of the actin cytoskeleton through latrunculin A treatment, Ssk2p concentrates in the neck of budding yeast cells and concurrently forms a 1:1 complex with actin. These observations suggest that Ssk2p has a novel, previously undescribed function in sensing damage to the actin cytoskeleton. We also describe a second function for Ssk2p in facilitating reassembly of a polarized actin cytoskeleton at the end of the cell cycle, a prerequisite for efficient cell cycle completion. Loss of Ssk2p, its kinase activity, or its ability to localize and interact with actin led to delays in actin recovery and a resulting delay in cell cycle completion. These unique capabilities of Ssk2p are activated by a novel mechanism that does not involve known components of the HOG pathway.

Indexed as

Osmotic PressureActinsBridged Bicyclo Compounds, HeterocyclicCell CycleCytoskeletonFluorescent DyesGenes, FungalMAP Kinase Kinase KinasesMAP Kinase Signaling SystemProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSodium ChlorideThiazolesThiazolidinesActinsBridged Bicyclo Compounds, HeterocyclicFluorescent Dyeslatrunculin AMAP Kinase Kinase KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSodium ChlorideSSK2 protein, S cerevisiaeThiazolesThiazolidines

Identifiers

PMID12181352
PMCPMC117948
OpenAlexW2167561185

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.