A role for Q/N-rich aggregation-prone regions in P-body localization.
J Cell Sci
; 121(Pt 15): 2463-72, 2008 Aug 01.
Article
in En
| MEDLINE
| ID: mdl-18611963
ABSTRACT
P-bodies are cytoplasmic foci that are sites of mRNA degradation and translational repression. It is not known what causes the accumulation of RNA-degradation factors in P-bodies, although RNA is required. The yeast Lsm1-7p complex (comprising Lsm1p to Lsm7p) is recruited to P-bodies under certain stress conditions. It is required for efficient decapping and degradation of mRNAs, but not for the assembly of P-bodies. Here we show that the Lsm4p subunit and its asparagine-rich C-terminus are prone to aggregation, and that this tendency to aggregate promotes efficient accumulation of Lsm1-7p in P-bodies. The presence of glutamine- and/or asparagine-rich (Q/N-rich) regions in other P-body components suggests a more general role for aggregation-prone residues in P-body localization and assembly. This is supported by reduced P-body accumulation of Ccr4p, Pop2p and Dhh1p after deletion of these domains, and by the observed aggregation of the Q/N-rich region from Ccr4p.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Asparagine
/
RNA, Messenger
/
Ribonucleoprotein, U4-U6 Small Nuclear
/
Cytoplasmic Granules
/
Saccharomyces cerevisiae Proteins
/
Glutamine
Language:
En
Journal:
J Cell Sci
Year:
2008
Type:
Article
Affiliation country:
United kingdom