Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mechanisms connecting the conserved protein kinases Kin1, Pom1, and Ssp1 in fission yeast cell polarity and division

ABSTRACT: Connections between the protein kinases that function within complex cell polarity networks are poorly understood. Rod-shaped fission yeast cells grow in a highly polarized manner, and genetic screens have identified many protein kinases required for polarized growth and cell shape. Kin1, the sole MARK/PAR-1 family kinase in fission yeast, regulates cell polarity and cytokinesis through unknown mechanisms. We performed a large-scale phosphoproteomics screen to identify and characterize Kin1 substrates in cells.

INSTRUMENT(S): Orbitrap Fusion, Q Exactive Plus

ORGANISM(S): Schizosaccharomyces Pombe (ncbitaxon:4896)

SUBMITTER: Arminja Kettenbach

PROVIDER: MSV000081185 | MassIVE | Thu Jun 22 11:24:00 BST 2017

SECONDARY ACCESSION(S): PXD006782

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Similar Datasets

Defining how Pak1 regulates cell polarity and cell division in fission yeast

Project description:For polarized growth of cells, protein kinases regulate the assembly of cytoskeletal structures at the correct time and place. Large cytoskeletal structures must also be assembled in a regulated manner during cytokinesis and cell separation. We performed a visual screen to identify cell polarity protein kinases that might also function in cytokinesis and cell separation. We found that the Cdc42-activated protein kinase Pak1 (also called Orb2 and Shk1) colocalizes with the assembling cytokinetic ring and remains in the cell middle during septation. Mutations in pak1 led to defects in cytokinetic ring assembly and cell separation, as well as previously known cell polarity defects. We performed a phosphoproteomic screen and identified novel Pak1 targets that were verified as direct substrates in vitro. Top targets included proteins that function in polarized growth, cytokinesis, and septation. For cytokinesis, we found that Pak1 regulates the localization of its substrates Mid1 and Cdc15 to the cell cortex and the cytokinetic ring. For cell separation, Pak1 phosphorylates the RNA-binding protein Sts5 to prevent its assembly into P-body granules. The cell separation defect of pak1 mutants was suppressed by a non-phosphorylatable sts5 mutant. These results show that Pak1 acts directly on components of the cytokinetic ring, but unexpectedly promotes the later stages of cell division by inhibiting the assembly of ribonucleoprotein granules. More broadly, our work reveals that cell polarity signaling proteins coordinate diverse events to promote cell division at the end of the cell cycle.

2019-07-02 | MSV000084047 | MassIVE

Identification of genes responsive to change in apical polarity in the breast epithelium

Project description:Differentiation of monolayered epithelia is characterized by the formation of a basoapical polarity axis, except during the early stages of cancer development. Using mammary glandular structures (acini) produced in a three-dimensional cell culture system we have demonstrated that, in order for mammary epithelial cells to exit quiescence and enter the cell cycle, acini have to lose apical polarity. In order to identify the genes dependent on apical polarity that could control cell quiescence, and possibly other aspects of tissue homeostasis, we have used Affymetrix technology microarray analysis of the 22,277 features/genes of the Human Genome U133A 2.0 array Chip in apically polarized and non-polarized breast epithelial acinar cells in three-dimensional culture. Genes commonly down-regulated in two treatments that altered apical polarity compared to control were considered to be dependent on apical polarity status for their transcription. Apically polarized (Control) and two different populations of non-polarized human mammary epithelial cells (18-alpha-glycyrrhetinic acid =AGA, and 5-aza-2'-deoxycytidine =Aza) were used for microarray analysis containing four biological replicates (1-4) for each treatment. The two treatments that cause loss of apical polarity were compared to reference apically polarized control samples using two different statistical analysis methods (FDR and HolmM-bM-^@M-^Ys).

2012-02-29 | E-GEOD-35165 | biostudies-arrayexpress

Fission yeast NDR/LATS kinase Orb6 regulates exocytosis via phosphorylation of exocyst complex

Project description:NDR/LATS kinases regulate multiple aspects of cell polarity and morphogenesis from yeast to mammals, but few of their substrates are known. Fission yeast NDR/LATS kinase Orb6 has been proposed to control cell polarity via spatial regulation of Gef1, a guanine nucleotide exchange factor for the small GTPase Cdc42. Here we show that Orb6 plays a critical role as a positive regulator of exocytosis, independent of Gef1. Through Orb6 inhibition in vivo and quantitative global phosphoproteomics, we identify several proteins involved in membrane trafficking as Orb6 targets, and we confirm Sec3 and Sec5, conserved components of the exocyst complex, as substrates of Orb6 both in vivo and in vitro. Our results suggest that Orb6 kinase activity is crucial for exocyst localization to actively-growing cell tips and for exocyst activity during septum dissolution after cytokinesis. We further show that Orb6 phosphorylation of Sec3 serine-201 contributes to exocyst function in parallel with exocyst protein Exo70. We propose that Orb6 contributes to polarized growth by regulating membrane trafficking at multiple levels.

2019-01-31 | PXD009408 | Pride

Identification of genes responsive to change in apical polarity in the breast epithelium

2012-02-29 | GSE35165 | GEO

Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease

Project description:Supporting data for Chen et al., "Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease" The microarray component of this work seeks to identify genes whose expression is controlled by the Caulobacter crescentus DivJ-PleC-DivK system. Keywords: time course, mutant/wild-type comparisons

2005-12-08 | GSE3144 | GEO

Time-resolved function of cell polarity kinases PRKCZ and PRKCI in CNS myelination [bulk_oligo]

Project description:The atypical Protein Kinase C (aPKC) is a critical component of the PAR polarity complex, as well as of cell polarity in general. There are two paralogs of aPKC in the mammalian genome. Their expression pattern and functional role in oligodendrocyte lineage differentiation and development remains heretofore uncharacterized. Here we show that both paralogs of aPKC – PRKCI, the primary transcript of Prkci and PKMz, an alternate transcript of Prkcz – are expressed during oligodendrocyte differentiation, yet are functionally non-redundant. Asymmetric cell division and early specification of the oligodendrocyte fate stage required both paralogs. By contrast, the stage of oligodendrocyte maturation involving membrane polarization and myelination of axons continued to require PKMz, but no longer needed PRKCI. Taken together, our results indicate to a two-stage role of aPKCs and cell polarity in oligodendrocyte differentiation and development.

2024-04-21 | GSE263979 | GEO

Time-resolved function of cell polarity kinases PRKCZ and PRKCI in CNS myelination [snrna_oligo]

2024-04-21 | GSE263981 | GEO

CDC42 controlled apical-basal polarity regulates intestinal stem cell to transit amplifying cell fate transition via YAP-EGF-mTOR signaling

Project description:Epithelial polarity is controlled by a polarity machinery including the Rho GTPase CDC42 and Scribble/PAR. By using intestinal stem cell (ISC)-specific deletion of CDC42 in Olfm4-IRES-eGFPCreERT2;CDC42flox/flox mice, we found that ISC-initiated CDC42 loss caused a drastic hyper-proliferation of transit amplifying (TA) cells and disrupted epithelial polarity. CDC42-null crypts displayed expanded TA cell and diminished ISC populations, accompanied by elevated hippo signaling via YAP/TAZ - Ereg and mTOR activation, independent from canonical Wnt signaling. YAP/TAZ conditional knockout restored the balance of ISC/TA cell populations and crypt proliferation but did not rescue the polarity in CDC42-null small intestine. mTOR or EGFR inhibitor treatment of CDC42 KO mice exhibited similar rescuing effects without affecting YAP/TAZ signaling. Inducible ablation of Scribble in intestinal epithelial cells mimics that of CDC42 KO defects including crypt hyperplasia and hippo signaling activation. Mammalian epithelial polarity regulates ISC and TA cell fate and proliferation via a hippo-Ereg-mTOR cascade.

2021-10-23 | GSE166736 | GEO

A survival mechanism controlled by cadherins and Dlg1 polarity complex inhibits Fas cell death receptor signaling

Project description:A fine regulation of epithelia cell death is required to maintain tissue integrity and homeostasis. At a cellular level, this life and death decision is controlled by environmental stimuli including death receptors activation. Here, we show that establishment of cell polarity and AJ formation control the pro-apoptotic signaling emanating from the death receptor Fas. We demonstrate that in colon epithelia Fas concentrates at cell-cell junctions together with the E-cadherin, which protects cells from FasL-induced cell death. The Fas-cadherin association requires the C terminal PDZ binding site of Fas and, using a proteomic approach, we showed that this domain allows the association with the polarity molecule Dlg1. We proved that the interaction of Fas with this scaffold molecule participate to this cell death protection. Therefore inhibition of FasL-induced cell death by Fas-cadherin-Dlg1 complex is a double-edged sword mechanism that helps to maintain epithelial homeostasis by (i) protecting normal polarized epithelia from apoptosis (ii) promoting the elimination of compromised non-polarized cells.

2018-09-20 | PXD009659 | Pride

Spatially resolved proteomics of the Arabidopsis stomatal lineage identifies polarity complexes for cell divisions and stomatal pores

Project description:Cell polarity is used to guide asymmetric divisions and create morphologically diverse cells. We find that two oppositely oriented cortical polarity domains present during the asymmetric divisions in the Arabidopsis stomatal lineage are reconfigured into polar domains marking ventral (pore-forming) and outward facing domains of maturing stomatal guard cells. Proteins that define these opposing polarity domains were used as baits in miniTurboID-based proximity labeling. Among differentially enriched proteins we find SOSEKIs and their effector ANGUSTIFOLIA, protein kinase CKII and LC8-type DYNEIN LIGHT CHAIN1 as polar scaffolds. Using AI-facilitated protein structure prediction models, we identify their potential interaction interfaces. Functional and localization analysis of polarity protein OPL2 and its newly discovered partners suggest a positive interaction with mitotic microtubules and a potential role in cytokinesis. This combination of cutting-edge proteomics and structural modeling with live cell imaging provides insights into how polarity is rewired in different cell types and cell cycle stages.

2024-03-21 | PXD050287 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data