Richard Gaber / Professor / Biochemistry, Molecular biology and Cell Biology / PhD. University of Wisconsin at Madison
r-gaber@northwestern.edu
(847) 491-5452
(847) 467-1422
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The main area of interest for my laboratory involves signaling through the molecular chaperone known as the Hsp90. We have recently discovered that a key role of the Hsp90 complex of proteins is to negatively regulate the cell's ability to respond to heat shock. Hsp90 and the cyclophilin, Cpr7, keep this signal transduction pathway repressed under non-stress conditions. In related studies, we discovered a new component of the Hsp90 complex, Cns1, that is essential for life in S. cerevisiae. Cns1, like certain other Hsp90-associated protiens contains multiple tetra-tricopeptide repeat (TPR) motifs and it is through these domains that the interactions between Hsp90 and Cns1 appear to depend. Our goal is to discover specific essential in vivo role(s) played by the Hsp90 complex with particular emphasis on the part played by Cns1.
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Wu B, Ottow K, Poulsen P, Gaber RF, Albers E, Kielland-Brandt MC. Competitive intra- and extracellular nutrient sensing by the transporter homologue Ssy1p. J Cell Biol. 2006 May 8;173(3):327-31. Epub 2006 May 1.

P. Poulsen, B. Wu, R. F. Gaber & M. C. Kielland-Brandt (2005). "Constitutive signal transduction by mutant Ssy5p and Ptr3p components of the SPS amino acid sensor system in Saccharomyces cerevisiae." Eukaryot Cell 4, 1116-24.

R.F. Gaber, K. Ottow, H.A. Andersen and M.C. Kielland-Brandt (2003). "Constitutive and hyperresponsive signaling by mutant forms of Saccharomyces cerevisiae amino acid sensor Ssy1." Eukaryotic Cell Oct. 2003: 922-929.

M. Tesic, J.A. Marsh, S.B. Cullinan and R.F. Gaber (2003). "Functional interactions between Hsp90 and the Co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae." The Journal of Biological Chemistry 278(35): 32692-32701.

R. L. Nakamura and R. F. Gaber (1998). "Approaches to studying ion channels using yeast genetics." Meth. Enz.

R. F. Gaber, J. A. Marsh, and H. M. Kalton (1998). "Cns1 is an essential protein associated with the Hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7(delta) cells." Mol. Cell. Biol. 18: 7353-9.

R. F. Gaber, A. A. Duina, and H. M. Kalton (1998). "Requirement for Hsp90 and a Cyp-40-type cyclophilin in negative regulation of the heat shock response." Biol. Chem. 273: 18974-8.

H. Liang , C. H. Ko, T. Herman, and R. F. Gaber (1998). "Trinucleotide insertions, deletions and point mutations in glucose transporters confer K+ uptake in Saccharomyces cerevisiae." Mol. Cell. Biol. 18: 926-935.

M. B. Wright, E. A. Howell, and R. F. Gaber (1997). "Amino acid substitutions in membrane-spanning domains of Hol1, a member of the major facilitator superfamily of transporters, confer nonselective cation uptake in Saccharomyces cerevisiae." J. Bact. 178: 7197-7205.

R. L. Nakamura, J. A. Anderson, and R. F. Gaber (1997). "Determination of key structural requirements of a K+ channel pore." J. Biol. Chem. 272: 1011-1018.

M. B. Wright, J. Ramos, M. J. Gomez, K. Moulder, M. Scherrer, G. Munson and R. F. Gaber (1997). "Potassium transport by amino acid permeases in Saccharomyces cerevisiae." J. Biol. Chem. 272: 13647-13652.

A. A. Duina, H.-C. J. Chang, J. A. Marsh, S. Lindquist, and R. F. Gaber (1996). "A Function for Cyclophilin in Hsp90-mediated Signal Transduction." Science 274: 1713-1715.

H. Liang and R. F. Gaber (1996). "A novel signal transduction pathway in Saccharomyces cerevisiae defined by Snf3-regulated expression of HXT6." Mol. Biol. Cell 7: 1953-1966.

A. A. Duina, J. A. Marsh, and R. F. Gaber (1996). "Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth." Yeast 12: 943-952.

View all publications by publications by Richard F. Gaber listed in the National Library of Medicine (PubMed).
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