Research Topics
| J L BrodskySummaryAffiliation: University of Pittsburgh Country: USA Publications
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Publications
Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulumJ L Brodsky
Department of Biological Sciences, University of Pittsburgh, PA 15260, USA
FEBS Lett 435:183-6. 1998..We conclude that mHsp70 is unable to support protein translocation into the ER because it fails to associate productively with Sec63p and a precursor...- The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinctJ L Brodsky
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
J Biol Chem 274:3453-60. 1999..We found that pro-alpha factor and A1PiZ were degraded normally, indicating further that import and export are distinct and that other cytosolic factors may pull polypeptides from the ER... - Mutations in the cytosolic DnaJ homologue, YDJ1, delay and compromise the efficient translation of heterologous proteins in yeastJ L Brodsky
Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260, USA
Biochemistry 37:18045-55. 1998..Statistical analysis of the FFLux, GFP, and TBP encoding genes suggests that Ydj1p facilitates the expression of proteins that are poorly translated because both FFLux and GFP contain an abundance of codons that are rarely used in yeast... - Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactionsJ L Brodsky
Department of Biological Sciences, University of Pittsburgh, PA 15260, USA
Biochem Pharmacol 57:877-80. 1999..Thus, the immunosuppressive and cytostatic effects of DSG may be specific for a subset of cellular Hsc70s and confined to DnaJ-independent Hsc70-mediated activities... 
Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulumA J McClellan
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
Genetics 156:501-12. 2000..Our data suggest that a productive interaction between Ssa1p and Ydj1p is required to promote protein translocation...- Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ERA J McClellan
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
Mol Biol Cell 9:3533-45. 1998..We conclude that a conformation- and ATP-dependent interaction of BiP with the J domain of Sec63p is essential for protein translocation and that the specificity of hsc70 action is dictated by their DnaJ partners... - Yeast ribosomes bind to highly purified reconstituted Sec61p complex and to mammalian p180M W Morrow
Department of Biological Sciences, University of Pittsburgh, 267 Crawford Hall, Pittsburgh, PA 15260, USA
Traffic 2:705-16. 2001..Despite this increase in ribosome binding, neither co- nor post-translational translocation was compromised in vivo. In sum, our data suggest that the Sec61p complex is a ribosome receptor in the yeast endoplasmic reticulum membrane... - Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeastY Zhang
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
Mol Biol Cell 12:1303-14. 2001.... - Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysisS W Fewell
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
J Biol Chem 276:910-4. 2001..Biochemical studies demonstrate that R/1 most likely exerts these effects by altering the oligomeric state of hsc70... - BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulumJ L Brodsky
Department of Biological Sciences, University of Pittsburgh, PA 15260, USA
Proc Natl Acad Sci U S A 92:9643-6. 1995..amp; Rapoport, T.A. (1993) Cell 75, 615-630], is not due to a distinction between cotranslational translocation in mammalian cells and posttranslational translocation in yeast cells... - Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradationJ L Goeckeler
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA
Diabetes Obes Metab 12:32-8. 2010..We will also indicate links between ERAD and disease and emphasize future research avenues... - Water transport across yeast vacuolar and plasma membrane-targeted secretory vesicles occurs by passive diffusionL A Coury
Laboratory of Epithelial Cell Biology, Renal Electrolyte Division, Department of Medicine, University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania 15213 2500, USA
J Bacteriol 181:4437-40. 1999..However, spheroplasts prepared from the strain overexpressing Fps1p showed enhanced glycerol uptake, suggesting that Fps1p becomes active only upon insertion in the plasma membrane... - The action of molecular chaperones in the early secretory pathwayS W Fewell
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
Annu Rev Genet 35:149-91. 2001..Molecular chaperones play critical roles in each of these phenomena... - Heat shock protein 101 effects in A. thaliana: genetic variation, fitness and pleiotropy in controlled temperature conditionsS J Tonsor
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA
Mol Ecol 17:1614-26. 2008..Hsp101 expression appears to carry an important trade-off in reduced root growth. This trade-off may select for suppressed expression under chronically high temperatures... 
Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradationS I Nishikawa
Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa ku, Nagoya 464 8602, Japan
J Cell Biol 153:1061-70. 2001..These results suggest that one role of the BiP, Jem1p, and Scj1p chaperones is to maintain lumenal ERAD substrates in a retrotranslocation-competent state...- A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposomeJ L Brodsky
Division of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley 94720
J Cell Biol 123:1355-63. 1993..We conclude that the purified Sec63p complex is active and required for protein translocation, and that the association of BiP with the complex may be regulated in vivo... - Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like proteinC H Leng
Institute of Molecular Biology, Academia Sinica, National Defense Medical Center, Taipei, Taiwan
Protein Sci 7:1186-94. 1998..The purified proteins stimulated the ATPase activity of hsc70 and of the 60-kDa N-terminal fragment of hsc70. These results imply that RDJ1 can interact with the N-terminal 60-kDa fragment of hsc70 to activate ATP hydrolysis by hsc70... - Recognition and delivery of ERAD substrates to the proteasome and alternative paths for cell survivalA A McCracken
Biology Department, University of Nevada, Reno, NV 89557, USA
Curr Top Microbiol Immunol 300:17-40. 2005..When the capacity of the ERAD machinery is exceeded or compromised, multiple degradative routes can be enlisted to prevent the detrimental consequences of ERAD substrate accumulation, which include cell death and disease...