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FRISC: The Faculty Research Interests Science Comparator |
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Professor of Pharmacology
Biological Chemistry
Cell Regulation
Office: (214) 648-2359
FAX: (214) 648-2994
Email: goodma02@utsw.swmed.edu
The broad interest of the
laboratory is protein trafficking within the cell and the assembly of
organelles. We focus on the biogenesis of peroxisomes in yeast.
Peroxisomes are found in virtually every eukaryote and catalyze many essential
reactions for the organism. Humans who cannot properly assemble
peroxisomes are born, miraculously, but die early in childhood as several organ
systems fail. It is thus clinically important to understand how this
organelle is normally assembled. Yeast is a good model system for this
purpose.
The outline of protein import
into the peroxisomal matrix (lumen) is becoming understood. Proteins
containing targeting sequences are recognized by soluble receptors, and
receptor-cargo complexes then dock on the peroxisomal surface, and translocation
ensues. The pathway for the assembly of peroxisomal membrane proteins is
more poorly understood.
Current projects in the
laboratory:
1) We have been studying
the targeting and assembly pathway of a model membrane protein termed Pmp47.
We have recently identified its targeting motif that directs it to peroxisomes.
We are performing screens to identify proteins that are important for the
targeting and assembly of Pmp47 into the membrane. At present we have
several interesting candidates, one of which is required for Pmp47 targeting,
and we are further characterizing its function.
2) We have discovered that
yeast contains two types of peroxisomes depending on the growth substrate.
Different regions of Pmp47 target the molecule to one or the other of these
organelle subtypes. We would like to understand the functions of these
organelles and how they are different regarding recognition of targeting
sequences.
3) In 1994 we discovered
that folded proteins and oligomers can cross the peroxisomal membrane.
However, peroxisomes lack visible pores. We would like to understand how
oligomeric import into peroxisomes occurs. We seek to understand the
architecture of the import complexes to know how they accommodate large folded
cargos.
4) In other work, we have begun to study the roles of
phosphatidylinositols in yeast. We have been characterizing a new PI-4
kinase that localizes to the yeast vacuole. We seek to understand its
function.
Selected Publications:
Wang, X., Ballard, J.L., Shelton,
S.N., and Goodman, J.M. Targeting signals on a peroxisomal membrane protein
distinguish basal from induced peroxisomes. Submitted
Stewart, M.Q., Esposito, R.,
Gowani, J.W., and Goodman, J.M. (2001) Alcohol oxidase and
dihydroxyacetone synthase, the abundant peroxisomal proteins of methylotrophic
yeasts, assemble in different cellular compartments. J. Cell Sci,
114:2863-2668
Wang, X., Unruh, M.J., and
Goodman, J.M. (2001) Discrete targeting signals direct Pmp47 to
oleate-induced peroxisomes in Saccharomyces
cerevisiae . J. Biol. Chem. 276:10897-10905
Marshall, P.A., Dyer, J.M.,
Quick, M.E., and Goodman, J.M. (1996) Redox-sensitive homodimerization of
peroxisomal Pmp27: A proposed mechanism to regulate organellar division.
J Cell Biol. 135:123-137
Dyer, J.M., McNew, J.A. and
Goodman, J.M. (1996) The sorting sequence of the peroxisomal integral
membrane protein PMP47 is contained within a hydrophilic loop. J. Cell
Biol. 133:269-280
McNew, J.A. and Goodman, J.M.
The targeting and assembly of peroxisomal proteins: Some old rules do not apply.
(1996) Trends Biochem. Sci. 21:54-58
Page maintained by Stephanie
Robertson
Last updated: 22 Aug 2001
Extraction Method: Expand using Medical Synonyms-
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