Protein Degradation in Development and Aging
Our laboratory uses the
nematode worm Caenorhabditis elegans as a model organismn
to study general regulatory aspects of the ubiquitin/proteasome
system (UPS) in developmental and aging processes. We currently have one
Postdoc or two PhD positions available and are looking for outstanding
candidates. Candidates should ideally already have been exposed to a
laboratory environment. While previous experience in C. elegans is not
necessary, this, or experience with a genetic system would certainly be a plus.
Selected
Literature:
The ubiquitin-selective
chaperone CDC-48/p97 links myosin assembly to human myopathy.
Janiesch
P.C., Kim J., Mouysset J., Barikbin
R., Lochmüller H., Cassata G., Krause S., and Hoppe
T. (2007). Nat. Cell Biol. (doi: 10.1038/ncb1554)
The UNC-45
Chaperone Mediates Sarcomere Assembly through Myosin
Degradation in C. elegans. Landsverk
M.L., Hutagalung A.H., Li S., Najafov
A., Hoppe T., Barral J.M., and Epstein H.F. (2007).
J. Cell Biol.
(in press)
A Conserved
Role of C. elegans CDC-48 in
ER-Associated Protein Degradation.
Mouysset
J., Kähler C., and Hoppe T. (2006). Journal Struct. Biol. 156, 41-49.
Multiubiquitylation
by E4 enzymes: one size doesn't fit all.
Hoppe T.
(2005). Trends Biochem. Sci. 30, 183-187.
Regulation
of the Myosin-Directed Chaperone UNC-45 by a Novel E3/E4-Multiubiquitylation
Complex in C. elegans. Hoppe
T., Cassata G., Barral J.M., Springer W., Hutagalung A.H., Epstein H.F., and Baumeister
R. (2004). Cell 118, 337-49.
To apply, please forward curriculum
vitae, bibliography, and the names and addresses of referees to:
Dr. Thorsten
Hoppe, Centre for Molecular Neurobiology Hamburg (ZMNH), Falkenried
94, 20251