The LSM domain-containing protein LSM14/Rap55 plays a role in mRNA decapping, translational repression, and RNA granule (P-body) assembly. How LSM14 interacts with the mRNA silencing machinery, including the eIF4E-binding protein 4E-T and the DEAD-box helicase DDX6, is poorly understood. ...
Pat1 is a key protein that functions in P body assem- bly, decapping activation and translational repression. It contains three domains: the N-terminal domain, the middle domain and the C-terminal domain in yeast [21] (Figure 1A). Pat1 has conserved interactions with Dcp2, Lsm1-7 ...
We identified a Sm-like protein Lsm12 complexed with NAADP, TPC1, and TPC2. Lsm12 directly binds to NAADP via its Lsm domain, colocalizes with TPC2, and mediates the apparent association of NAADP to isolated TPC2 or TPC2-containing membranes. Lsm12 is essential and immediately participates...
Future experiments will have to show whether the Lsm protein is more directly involved in the regulation of motility or whether the deletion of the Sm1 domain affects a downstream regulator like for instance a small regulatory sRNA. Regulation of mobility genes by sRNAs might be possible since it...
E. Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24. RNA 16, 792–804 (2010) Article CAS Google Scholar Martin-Tumasz, S., Richie, A. C., Clos, L. J., II, Brow, D. A. & Butcher, S. E. A novel occluded RNA ...
and D3 decisively influences their binding to the Tudor domain of the "survival of motor neurons" protein (SMN): inhibition of dimethylation by S-adenosylhomocysteine (SAH) abolished the binding of D1, D3, B/B', and LSm4 to this domain. A synth...
Protein & Cell(2019) Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation Donghui Wu Denise Muhlrad Haiwei Song Cell Research(2014) mRNA-based therapeutics — developing a new class of drugs
Cover slips containing the cells were then washed by PBS-TX (10 mL PBS+10 μL 10% Tri- tonx-100) three times and mounted using mounting medium (PBS: Glycerol=1:1 v/v) and analyzed by fluorescence micros- copy (Leica DM IRB). Acta Pharmacologica Sinica www.chinaphar.com Li L et ...
In addition, RNAs accumulate in the cytoplasm due to the lack of the C-terminal Q/N-rich domain of KlLSM4 that is needed for efficient RNA degradation [7,8] and for P-bodies localization [9,10]. The expression of the truncated S. cerevisiae protein in the absence of LSM4 recapitulated...