INVESTIGADORES
MUÑOZ Manuel Javier
artículos
Título:
The Serine-Arginine Rich Protein SF2/ASF Regulates Protein SUMOylation
Autor/es:
PELISCH F; GEREZ J; DRUKER J; SCHOR IE; MUÑOZ MJ; RISSO G; PETRILLO E; WESTMAN BJ; LAMOND AI; ARZT E; SREBROW A.
Revista:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Editorial:
NATL ACAD SCIENCES
Referencias:
Año: 2010 vol. 107 p. 16119 - 16124
ISSN:
0027-8424
Resumen:
Abstract
A role for SUMOylation in the
biogenesis and/or function of Box C/D snoRNPs has been reported,
mediated via SUMO2 conjugation to the core snoRNP protein, Nop58. A
quantitative proteomics screen, based on SILAC (stable-isotope labeling
by amino acids in cell culture) and mass spectrometry using extracts
prepared from cultured mammalian cells expressing either 6His-SUMO1 or
-SUMO2, revealed that the snoRNP-related proteins Nop58, Nhp2, DKC1 and
NOLC1 are amongst the main SUMO-modified proteins in the nucleolus.
SUMOylation of Nhp2 and endogenous Nop58 was confirmed using a
combination of in vitro and cell-based assays and the modified lysines
identified by site-directed mutagenesis. SUMOylation of Nop58 was found
to be important for high-affinity Box C/D snoRNA binding and the
localization of newly transcribed snoRNAs to the nucleolus. Here, these
findings are reviewed and a model for understanding Nop58 SUMOylation in
the context of Box C/D snoRNP biogenesis is presented. Given the
essential role of snoRNPs in the modification of pre-ribosomal RNA, this
work suggests that SUMO, snoRNPs and ribosome assembly, and thus
cellular translation, growth and proliferation, may be linked via novel
mechanisms which warrant further investigation.