Dataset: Role of Phosphatases in the Regulation of Mitotic Exit, 2016

Abstract

In “Role of Phosphatases in the Regulation of Mitotic Exit, 2016” we investigated the regulation of cell division. Tight control of this process is essential, and failure to do so can lead to cancer. For many years, the focus of attention has been laid in a group of proteins known as Cyclin-dependent kinases, which work as an engine to drive cell division. These kinases are able to modify other proteins in order to change their function or activity. However, a different sort of proteins known as protein phosphatases can revert the action of these kinases, and hence can also have a major role in controlling cell division. We centered our studies on one of them: PP2A. We found that it is a central component in the regulation of cell division and differentiation, especially in conditions of nutritional stress.  

Five datasets are attached to this project:

Data title: PP2A-Pab1 interacting proteins. Proteomic analysis of protein associated to PP2A-Pab1. Pab1 was tagged with an N-terminal tag that was used to pull it down from fission yeast native extracts. Associated proteins were analyzed by tandem mass spectrometry.

Data title: Phosphoproteomic analysis of yeast extracts in cells depleted of PP2A-Pab1. Phosphoproteomic analysis of proteins whose phosphorylation changes upon depletion of PP2A-Pab1.

Data title: Analysis of RNA expression changes in a pab1 deletion mutant in response to nitrogen starvation. Excel file comparing RNA sequencing data. Comparison of RNA expression in a pab1 deleted strain before and after nitrogen starvation treatment (for 4 h).

Data title: Mating counting of different yeast mutants. Excel file containing mating counting as a mean to determine cell differentiation. Different homotallic yeast strains containing different mutations were analyzed regarding their ability to undergo sexual differentiation.

Data title: Real time PCR analysis of mei2 expression in several mutant strains. Excel file containing real time PCR data of mei2 expression normalized to actin expression. Different yeast strain were grown at permissive or at restrictive temperature and the levels of mei2 expression were analysed by RT-PCR


For access to the dataset, use the NSD application form:  

http://www.nsd.uib.no/nsd/english/orderform.html

Variable Groups

Full Title

Role of Phosphatases in the Regulation of Mitotic Exit, 2016

Identification Number

NSD2412

Authoring Entity

Name Affiliation
Lopez-Aviles, Sandra Centre for Molecular Medicine Norway, University of Oslo

Producer

Name Affiliation Abbreviation Role
Lopez-Aviles, Sandra Centre for Molecular Medicine Norway, University of Oslo UiO Principal Investigator

Copyright

Copyright (C) 2016 Sandra Lopez-Aviles, UiO

Funding Agency/Sponsor

Name Abbreviation Role Grant
The Research Council of Norway RCN 214049
University of Oslo

Data Distributor

Name Affiliation Abbreviation
NSD – Norwegian Centre for Research Data NSD

Version

Date: 2017-06-02

Notes

Original data from Sandra Lopez-Aviles, UiO are documented and prepared, first NSD-version.

Bibliographic Citation

"Role of Phosphatases in the Regulation of Mitotic Exit, 2016". Data collected by Sandra Lopez-Aviles, UiO. First NSD edition, Bergen 2017.

List of Keywords

Topic Classification

Time Period Covered

Start End Cycle
2012 2015

Date of Collection

Start End Cycle
2014-07-01 2014-12-12
2015-01-02 2015-05-21
2015-01-02 2015-07-08
2014-01-02 2016-05-01
2015-11-13 2016-05-25

Country

Norway  (NO)

Unit of Analysis

Other

Universe

Proteomic analysis of protein associated to PP2A-Pab1, phosphoproteomic analysis, analysis of RNA expression changes in a pab1 deletion mutant in response to nitrogen starvation, mating counting of different yeast mutants and excel files containing real time PCR data of mei2 expression normalized to actin expression.

Kind of Data

Other

Time Method

Cross-sectional survey

Data Collector

Lopez-Aviles, Sandra, Centre for Molecular Medicine Norway, University of Oslo  (UiO)

Sampling Procedure

Data title: PP2A-Pab1 interacting proteins. Proteomic analysis of protein associated to PP2A-Pab1. Pab1 was tagged with an N-terminal tag that was used to pull it down from fission yeast native extracts. Associated proteins were analyzed by tandem mass spectrometry. Tandem affinity purification followed by protein digestion and MS-MS analysis. Sample obtained from yeast cultures of a strain expressing TAP-Pab1. Culture size: 2 l of an optical density of 0,5.  

Data title: Phosphoproteomic analysis of yeast extracts in cells depleted of PP2A-Pab1. We created a strain where PP2A-Pab1 activity could be inhibited by the addition of thiamine and auxin to the medium. Cultures of this strain were either treated or mock treated with auxin and thiamine, and changes in the phosphorylation profile was analysed by phosphopetide enrichment followed by mass spectrometry analysis. Sample obtained from yeast cultures of a strain expressing nmt41-miniAID pab1. Culture size: 100ml of an optical density of 0,5.

Data title: Analysis of RNA expression changes in a pab1 deletion mutant in response to nitrogen starvation. A pab1-deleted strain was exposed to nitrogen starvation or grown in nitrogen rich medium for 4h. Samples were collected and RNA was extracted. After library construction, the samples were analysed using RNA-sequencing (NextSeq 500 75 bp SR H.O). Sample obtained from yeast cultures of a pab1-deleted strain. Culture size: 20ml of an optical density of 0,4.  

Data title: Mating counting of different yeast mutants. Yeast cultures containing 0,5x10^6 cells/ml were exposed to nitrogen starvation and their ability to undergo sexual differentiation was evaluated based on the counting of tetrads and zygotes in the culture. Different yeast mutant strains. Culture size: 5 ml.

Data title: Real time PCR analysis of mei2 expression in several mutant strains. Different yeast strain were grown at permissive or at restrictive temperature. 20 ml samples were collected and RNA was extracted. Following cDNA amplification, mei2 expression was determined using real time PCR. 20 ml cultures of O.D 0,3.

Mode of Data Collection

Other

Location

Availability Status

Data from "Role of Phosphatases in the Regulation of Mitotic Exit, 2016" are made available for research, teaching and students when ordered.

Extent of Collection

20 data files; different formats can be made.

Restrictions

Data from "Role of Phosphatases in the Regulation of Mitotic Exit, 2016" are made available for research, teaching and students when ordered.

Citation Requirement

Users are obliged to refer to producer and distributor of the data by writing the following in forewords or footnotes in eventual publications:
"(Some of) the data applied in the analysis in this publication are based on "Role of Phosphatases in the Regulation of Mitotic Exit, 2016". The survey was financed by The Reasearch Council of Norway. The data are provided by Sandra Lopez-Aviles, UiO and prepared and made available by NSD – Norwegian Centre for Research Data. Neither Sandra Lopez-Aviles, UiO, The Research Council of Norway nor NSD are responsible for the analysis/interpretation of the data presented here.

Deposit Requirement

Access to data is given on the condition that NSD gets a PDF-file of eventual reports that are written on the basis of the data. This to ensure best possible information of the use of data we distribute.

Conditions

The order form has to include name, institutional affiliation, project title, information about sources of financing and postal address. A declaration of secrecy has to be signed before delivery of data.

Disclaimer

Neither Sandra Lopez-Aviles, UiO, The Research Council of Norway nor NSD are responsible for the analysis/interpretation of the data presented here.

Related Publications

A PP2A-B55-Mediated Crosstalk between TORC1 and TORC2 Regulates the Differentiation Response in Fission Yeast

Martin, R., Portantier, M. et al. (2017)  A PP2A-B55-Mediated Crosstalk between TORC1 and TORC2 Regulates the Differentiation Response in Fission Yeast, in: Current Biology, 27: p. 175-188.

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