... as a GET body scaffold. Systematic compositional analyses of GET bodies reveal their chaperone-rich nature and the presence of numerous proteins involved in metabolic processes. Temporal analyses of GET body assembly demonstrate the sequential recruitment of different chaperones, and we discover...

... is promoted by the Hsp90–Cdc37 chaperone complex. Our results show that atp2 Δ cdc28td double-mutant cells, but not single mutants, are sensitive to chemical inhibition of the Hsp90–Cdc37 complex, and exhibit reduced levels of additional Hsp90–Cdc37 client kinases, suggesting an inhibition of this complex...

...Helena M. Schnell; Richard M. Walsh, Jr.; Shaun Rawson; John Hanna ABSTRACT Much of cellular activity is mediated by large multisubunit complexes. However, many of these complexes are too complicated to assemble spontaneously. Instead, their biogenesis is facilitated by dedicated chaperone proteins...

...Sophie Dittmer; Tatjana Kleine; Serena Schwenkert ABSTRACT Molecular chaperones play an important role during the response to different stresses. Since plants are sessile organisms, they need to be able to adapt quickly to different conditions. To do so, plants possess a complex chaperone machinery...

... by structurally related α- and β-subunits. CP biogenesis typically begins with the assembly of the α-ring, which then provides a template for β-subunit integration. In eukaryotes, α-ring assembly is partially mediated by two hetero-dimeric chaperones, termed Pba1–Pba2 (Add66) and Pba3–Pba4 (also known as Irc25...

...-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones . J. Cell Sci.   120 , 1743 - 1751 . 10.1242/jcs.002410 Adamus , G. , Zam , Z. S. , Arendt , A. , Palczewski , K. , McDowell , J. H. and Hargrave , P. A. (1991). Anti...

...Ganapathi Kandasamy; Claes Andréasson ABSTRACT During protein quality control, proteotoxic misfolded proteins are recognized by molecular chaperones, ubiquitylated by dedicated quality control ligases and delivered to the 26S proteasome for degradation. Proteins belonging to the Hsp70 chaperone...

...) in stressed cells. Owing to its multi-domain structure, it engages in diverse processes that are crucial for proteome maintenance. BAG3 promotes the activity of molecular chaperones, sequesters and concentrates misfolded proteins, initiates autophagic disposal, and balances transcription, translation...

... are present, newly formed aggregates make a relatively small contribution to total aggregate load, and thus the impact of HspB7 is lost. Although HspB7 affected a pre-aggregated structure, surprisingly, the chaperone did not prevent aggregate growth. This implies that HspB7 either affects newly formed...

...Bum-Chan Park; Yang-In Yim; Xiaohong Zhao; Maciej B. Olszewski; Evan Eisenberg; Lois E. Greene ABSTRACT Cyclin-G-associated kinase (GAK), the ubiquitously expressed J-domain protein, is essential for the chaperoning and uncoating of clathrin that is mediated by Hsc70 (also known as HSPA8). Adjacent...

...Marina Serna; Gerardo Carranza; Jaime Martín-Benito; Robert Janowski; Albert Canals; Miquel Coll; Juan Carlos Zabala; José María Valpuesta Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). Whereas tubulin heterodimer formation is well‐characterized...

... an unknown mechanism. Herein, we show that mutations in SHP1 cause misfolding of Glc7 that co-aggregates with Hsp104 and Hsp42 chaperones and requires the proteasome for clearance. Mutation or depletion of the PP1 regulatory subunits Sds22 and Ypi1, which are involved in nuclear targeting of Glc7, also...

... epithelial cell culture system. We show a novel association between the leucine-rich repeat domain of Scrib and the co-chaperone Sgt1 and demonstrate that these proteins are necessary for epithelial morphogenesis and tubulogenesis following hepatocyte growth factor (HGF) stimulation. The molecular chaperone...

...Chi F. Lee; Girish C. Melkani; Qin Yu; Jennifer A. Suggs; William A. Kronert; Yoko Suzuki; Lori Hipolito; Maureen G. Price; Henry F. Epstein; Sanford I. Bernstein UNC-45 is a chaperone that facilitates folding of myosin motor domains. We have used Drosophila melanogaster to investigate the role...

... of the endoplasmic reticulum (ER), its increase did not result in significant accumulation of unfolded protein in the ER. Instead, ER chaperones and folding enzymes reached maximum synthesis rates immediately after TSH stimulation, before significant upregulation of Tg synthesis. The resulting increase in folding...

... of tail-anchored proteins at the endoplasmic reticulum. ‡ Authors for correspondence ([email protected] ; [email protected]) * These authors contributed equally to this work © The Company of Biologists Limited 2009 2009 Chaperone Endoplasmic reticulum...

... in a cytosolic staining pattern in pex19 cells only when co-expressed with Pex19p and were then localized to peroxisomes in a temporally differentiated manner. Pex19p probably functions as a chaperone for membrane proteins and transports them to peroxisomes by anchoring to Pex3p using residues 12-73 and 40-131...

... pellucida. Phosphoproteome analysis yielded the first evidence of molecular chaperones, endoplasmin (erp99) and heat shock protein 60 (hsp60), as targets for phosphorylation on the surface of mouse spermatozoa, whereas immunofluorescence localised these proteins to the precise region of the sperm head...

... 2003 © The Company of Biologists Limited 2004 2004 References Arai, H. and Atomi, Y. (1997). Chaperone activity of αB-crystallin suppresses tubulin aggregation through complex formation. Cell Struct. Funct. 22 , 539 -544. Atomi, Y., Yamada, S. and Nishida, T. (1991a). Early...

...+ ATPase with the β-subunit of the Na + /K + and H + /K + ATPases. Ca 2+ ATPase Na + /K + ATPase ATPase β-subunit Chaperone © The Company of Biologists Limited 2003 2003 27 1 2003 * Author for correspondence (e-mail: [email protected]) References Ackermann...