Staff Homepage

Dr Peter Fantes

Location: Darwin 413
Telephone:Office 650 5669
Lab 650 8693
Fax 650 8650

Email:P.Fantes@ed.ac.uk
Web-Site:

Photo of Peter Fantes

C.V.

PhD, Leicester University, 1972
Postdoctoral Research Assistant, Microbiology Department, Federal Institute of Technology, Zurich, Switzerland, 1972-74
Research Fellow in Department of Zoology, University of Edinburgh, 1974-79, with personal fellowships from:
- Royal Commission for the Exhibition of 1851
- Cancer Research Campaign
- Senior Research Fellowship in Basic Biomedical Science, Wellcome Trust.
Lecturer in Department of Zoology, University of Edinburgh, 1979-89
Reader; Department of Zoology, University of Edinburgh, 1989
Moved to Institute of Cell and Molecular Biology, now Institute of Cell Biology, 1990

Research groupings

Institute of Cell Biology

Teaching

Genes & Gene Action 2
Molecular Cell Biology 3
Genetic Approaches 4
Genetics Data Interpretation 4
Genetics 4:The Cell Cycle: DNA replication, segregation and checkpoints
Director of Studies

Research interests

Cell cycle control, stress responses, and chaperone function in fission yeast.

The fission yeast Schizosaccharomyces pombe has proved an excellent model system for cell cycle control and stress responses. The core of one stress-responsive pathway consists of a MAP kinase cascade which we and others investigated. In addition to regulating the expression of downstream genes, the pathway is involved in regulating cell cycle progress, primarily at the G2-mitosis boundary.

More recently we have turned to study the role of a molecular chaperone, Cdc37, which is conserved in fungi and animals. Molecular chaperones are involved in a variety of processes concerned with the folding, unfolding and stabilization of target or “client” proteins, and some are concerned with dealing with externally imposed stresses.

In other organisms the main clients of Cdc37 are specific protein kinases, and we have shown that the key cell cycle regulatory cyclin-dependent kinase (CDK) Cdc2 is a Cdc37 client in fission yeast. The mechanism by which Cdc37 acts on Cdc2 is being investigated. Other candidate client proteins have been identified and are being characterized.

In higher organisms Cdc37 associates stably with another chaperone Hsp90, which has a variety of roles in signal transduction. We have shown that in fission yeast Cdc37 and Hsp90 interact in high molecular weight complexes, but that under appropriate conditions the interaction is not essential for viability, although the proteins are individually essential. This suggests that the two chaperones share some functions while acting independently for others.

Representative publications

Turnbull EL, Martin IV, and Fantes PA (2005) Cdc37 maintains cellular viability in S. pombe independently of interactions with Hsp90. FEBS Journal 272: 4129-40

Turnbull EL, Martin IV, and Fantes PA (2005) The activity of Cdc2 and its interaction with the cyclin Cdc13 are dependent on the molecular chaperone Cdc37 in S. pombe. Journal of Cell Science, submitted for publication

Westwood PK, Martin IV, and Fantes PA (2004) Fission yeast Cdc37 is required for multiple cell cycle functions. Molecular Genetics and Genomics 271:82-90

Prochnik S, Fantes P (2001) Hyperthermotolerant fission yeast mutations, sow1 and sow2, suppress the cell cycle defect and stress sensitivity of MAP kinase kinase wis1?. Yeast:18:229-238

Samejima I, Mackie S, Warbrick E, Weisman R, Fantes PA (1998) The fission yeast mitotic regulator win1+ encodes a MAP kinase kinase kinase that phosphorylates and activates Wis1 MAP kinase kinase in response to high osmolarity.Molecular Biology of the Cell 9:2325-2335

Samejima I, Mackie S, Fantes PA (1997) Multiple modes of activation of the stress-responsive MAP kinase pathway in fission yeast. EMBO Journal 16:6162-6170

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