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Proteasomes
are large, multi-subunit complexes that act as the proteolytic core
of the ubiquitin-dependent protein degrading machinery, and are
responsible for the removal of abnormal polypeptides and short lived
regulatory proteins
from eukaryotic cells. Recent work, using the tools of biochemistry
and cell biology, has revealed much about the physical and biochemical
properties of proteasomes, but many aspects of their biological
function remain unclear.
As
an approach toward learning more about the role of proteasome-mediated
proteolysis during metazoan development, my lab has initiated a
genetic and molecular study of Drosophila proteasomes. Our
work is focused on two major questions:
- What
is the role of the ubiquitin-proteasome pathway in specific developmental
processes?
- Are
there structurally distinct cell-type specific proteasomes that
have specialized functions?
To
address the first question we have taken a mutational approach.
We have isolated and characterized two dominant temperature-sensitive
proteasome mutants (DTS5 and DTS7) that can be used to disrupt proteasome
function in vivo, and are using them to examine their effects on
specific biological processes.
For
the second question, we have used a reverse genetics approach. We
have identified and characterized five proteasome subunit genes
that are expressed exclusively in the male germline. A combination
of molecular, cell biological, and genetic approaches are being
used to investigate the importance of proteasome-mediated protein
degradation in spermatogenesis, and to address the functional role
of the testes-specific subunits in this process.
Undergraduate
students: Please click here
for information about research opportunities
in my lab. |
