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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