Quantitative analysis of human ras localization and function in the fission yeast Schizosaccharomyces pombe. Issue 4 (20th March 2013)
- Record Type:
- Journal Article
- Title:
- Quantitative analysis of human ras localization and function in the fission yeast Schizosaccharomyces pombe. Issue 4 (20th March 2013)
- Main Title:
- Quantitative analysis of human ras localization and function in the fission yeast Schizosaccharomyces pombe
- Authors:
- Bond, Michael
Croft, Wayne
Tyson, Richard
Bretschneider, Till
Davey, John
Ladds, Graham - Abstract:
- <abstract abstract-type="main"> <title>Abstract</title> <p>Ras signalling is central to fundamental and diverse cellular processes. In higher eukaryotes ras signalling is highly complex, involving multiple isoforms, regulatory proteins and effectors. As a consequence, the study of ras activity in mammalian systems presents a number of technical challenges. The model organism <italic>Schizosaccharomyces pombe</italic> has previously proved a key system for the study of human signalling components and provides an ideal model for the study of ras, as it contains just one ras protein (Ras1p), which is non‐essential and controls a number of downstream processes. Here we present data demonstrating the quantitative analysis of three distinct Ras1‐related signalling outputs, utilizing the three most abundant human ras isoforms, H‐Ras, N‐Ras and K‐Ras4B, in <italic>Sz. pombe</italic>. Further, we have characterized the localization of these three human ras isoforms in <italic>Sz. pombe</italic>, utilizing quantitative image analysis techniques. These data indicate that all three human ras isoforms are functional in fission yeast, displaying differing localization patterns which correlate strongly with function in the regulation of pheromone response and cell shape. These data demonstrate that such yeast strains could provide powerful tools for the investigation of ras biology, and potentially in the development of cancer therapies. Copyright © 2013 John Wiley &amp; Sons, Ltd.</p><abstract abstract-type="main"> <title>Abstract</title> <p>Ras signalling is central to fundamental and diverse cellular processes. In higher eukaryotes ras signalling is highly complex, involving multiple isoforms, regulatory proteins and effectors. As a consequence, the study of ras activity in mammalian systems presents a number of technical challenges. The model organism <italic>Schizosaccharomyces pombe</italic> has previously proved a key system for the study of human signalling components and provides an ideal model for the study of ras, as it contains just one ras protein (Ras1p), which is non‐essential and controls a number of downstream processes. Here we present data demonstrating the quantitative analysis of three distinct Ras1‐related signalling outputs, utilizing the three most abundant human ras isoforms, H‐Ras, N‐Ras and K‐Ras4B, in <italic>Sz. pombe</italic>. Further, we have characterized the localization of these three human ras isoforms in <italic>Sz. pombe</italic>, utilizing quantitative image analysis techniques. These data indicate that all three human ras isoforms are functional in fission yeast, displaying differing localization patterns which correlate strongly with function in the regulation of pheromone response and cell shape. These data demonstrate that such yeast strains could provide powerful tools for the investigation of ras biology, and potentially in the development of cancer therapies. Copyright © 2013 John Wiley &amp; Sons, Ltd.</p> </abstract> … (more)
- Is Part Of:
- Yeast. Volume 30:Issue 4(2013:Apr.)
- Journal:
- Yeast
- Issue:
- Volume 30:Issue 4(2013:Apr.)
- Issue Display:
- Volume 30, Issue 4 (2013)
- Year:
- 2013
- Volume:
- 30
- Issue:
- 4
- Issue Sort Value:
- 2013-0030-0004-0000
- Page Start:
- 145
- Page End:
- 156
- Publication Date:
- 2013-03-20
- Subjects:
- Yeast -- Periodicals
Yeasts -- Periodicals
Yeasts -- genetics -- Periodicals
Electronic journals
547 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/yea.2949 ↗
- Languages:
- English
- ISSNs:
- 0749-503X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9417.976000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4334.xml