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J. Cell Biol. Feb (2008); 180(3):579-95
The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery-
Boulon S, Marmier-Gourrier N, Pradet-Balade B, Wurth L, Verheggen C, Jady BE, Rothe B, Pescia C, Robert MC, Kiss T, Bardoni B, Krol A, Branlant C, Allmang C, Bertrand E, Charpentier B
Institute of Molecular Genetics of Montpellier, Centre National de la Recherche Scientifique, Unite Mixte de Recherche 5535, Montpellier Cedex 5, France-
Abstract: RNA-binding proteins of the L7Ae family are at the heart of many essential ribonucleoproteins -RNPs-, including box C-D and H-ACA small nucleolar RNPs, U4 small nuclear RNP, telomerase, and messenger RNPs coding for selenoproteins- In this study, we show that Nufip and its yeast homologue Rsa1 are key components of the machinery that assembles these RNPs- We observed that Rsa1 and Nufip bind several L7Ae proteins and tether them to other core proteins in the immature particles- Surprisingly, Rsa1 and Nufip also link assembling RNPs with the AAA - adenosine triphosphatases hRvb1 and hRvb2 and with the Hsp90 chaperone through two conserved adaptors, Tah1-hSpagh and Pih1- Inhibition of Hsp90 in human cells prevents the accumulation of U3, U4, and telomerase RNAs and decreases the levels of newly synthesized hNop58, hNHP2, 15-5K, and SBP2- Thus, Hsp90 may control the folding of these proteins during the formation of new RNPs- This suggests that Hsp90 functions as a master regulator of cell proliferation by allowing simultaneous control of cell signaling and cell growth-
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.