Результаты исследований: Научные публикации в периодических изданиях › статья
RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils. / Zaarur, N.; Xu, X.; Lestienne, P.; Meriin, A.B.; McComb, M.; Costello, C.E.; Newnam, G.P.; Ganti, R.; Romanova, N.V.; Shanmugasundaram, M.; Silva, S.T.; Bandeiras, T.M.; Matias, P.M.; Lobachev, K.S.; Lednev, I.K.; Chernoff, Y.O.; Sherman, M.Y.
в: EMBO Journal, Том 34, № 18, 2015, стр. 2363-2382.Результаты исследований: Научные публикации в периодических изданиях › статья
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TY - JOUR
T1 - RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils
AU - Zaarur, N.
AU - Xu, X.
AU - Lestienne, P.
AU - Meriin, A.B.
AU - McComb, M.
AU - Costello, C.E.
AU - Newnam, G.P.
AU - Ganti, R.
AU - Romanova, N.V.
AU - Shanmugasundaram, M.
AU - Silva, S.T.
AU - Bandeiras, T.M.
AU - Matias, P.M.
AU - Lobachev, K.S.
AU - Lednev, I.K.
AU - Chernoff, Y.O.
AU - Sherman, M.Y.
PY - 2015
Y1 - 2015
N2 - The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome-like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin-1 interacted directly with the RuvbL1 barrel-like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes se
AB - The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome-like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin-1 interacted directly with the RuvbL1 barrel-like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes se
KW - RuvbL
KW - aggresome
KW - amyloid
KW - disaggregation
U2 - 10.15252/embj.201591245
DO - 10.15252/embj.201591245
M3 - Article
VL - 34
SP - 2363
EP - 2382
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 18
ER -
ID: 3927728