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Genomes and Genes | Jason C YoungSummaryCountry: Germany Publications
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Publications
More than folding: localized functions of cytosolic chaperonesJason C Young
Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152, Martinsried, Germany
Trends Biochem Sci 28:541-7. 2003..Such flexibility is unique to the cytosolic Hsp70 and Hsp90 chaperone system...- Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchangeYasuhito Shomura
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Mol Cell 17:367-79. 2005..In contrast, BAG-1 and GrpE trigger a conserved conformational change in lobe II of the ATPase domain. Thus, nucleotide exchange on eukaryotic Hsp70 occurs through two distinct mechanisms... 
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone systemAlexander Brychzy
Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
EMBO J 22:3613-23. 2003..We propose a novel mechanism in which Tpr2 mediates the retrograde transfer of substrates from Hsp90 onto Hsp70. At normal levels substoichiometric to Hsp90 and Hsp70, this activity optimizes the function of the multichaperone machinery...- A stress sensor for the bacterial periplasmJason C Young
Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
Cell 113:1-2. 2003..This interaction relieves the inhibition of the neighboring protease domain of DegS, triggering a proteolysis cascade that leads to the sigma(E)-driven expression of periplasmic chaperones... - Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70Jason C Young
Cellular Biochemistry, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
Cell 112:41-50. 2003..We outline a novel mechanism in which chaperones are recruited for a specific targeting event by a membrane-bound receptor... - Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiaeHolger Sondermann
Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
J Biol Chem 277:33220-7. 2002..Thus, Snl1p is the first Bag domain protein identified in S. cerevisiae, and its interaction with Hsp70 is essential for biological activity... - Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperonesBenjamin M Abell
Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK
J Cell Sci 120:1743-51. 2007..On the basis of this in vitro analysis, we conclude that this chaperone pair can efficiently facilitate the ATP-dependent integration of TA proteins... - Pathways of chaperone-mediated protein folding in the cytosolJason C Young
Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec H3G 1Y6, Canada
Nat Rev Mol Cell Biol 5:781-91. 2004.... 
Functional divergence between co-chaperones of Hsc70Stefan Tzankov
Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada
J Biol Chem 283:27100-9. 2008..These results suggest a more complex model of Hsc70 mechanism than has been previously thought, with notable functional divergence between Hsc70 co-chaperones...- Essential role of the unusual DNA-binding motif of BAG-1 for inhibition of the glucocorticoid receptorUlrike Schmidt
Max Planck Institute of Psychiatry, Kraepelinstrasse 10, D-80804 Munich, Germany
J Biol Chem 278:4926-31. 2003..Thus, DNA binding and hsp70 interaction are required in cis. We propose that the nonsequence-specific DNA-binding protein BAG-1 acts at specific chromosomal loci by interacting with other proteins... - Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial importAnna C Y Fan
Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada
J Biol Chem 281:33313-24. 2006..This suggests a novel active role for Hsp90 in import steps subsequent to Tom70 targeting. Our results outline the mechanisms of Hsp90 function in preprotein targeting and transport... - Chaperones and transcriptional regulation by nuclear receptorsJason C Young
Nat Struct Biol 9:640-2. 2002 - Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial importMelanie K Bhangoo
Department of Biochemistry, McGill University, Montreal, QC, H3G 1Y6, Canada
Mol Biol Cell 18:3414-28. 2007..The Hsp90 cochaperones p23 and Aha1 also regulated Hsp90-preprotein interactions. We suggest that multiple cochaperones with similar yet partially specialized properties cooperate in optimal chaperone-preprotein complexes... - Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90Gabriela M Wochnik
Max Planck Institute of Psychiatry, Kraepelinstrasse 10, D-80804 Munich, Germany
FEBS Lett 560:35-8. 2004..Importantly, similar results were obtained with a constitutively active GR. Thus, the action of p23 on the nuclear stage of GR regulation requires its Hsp90 co-chaperone function, but not its chaperone activity...