MassIVEapplication/xmlftp://massive-ftp.ucsd.edu/v01/MSV000081830/primary200OK0000Anne-Claude Gingrashttps://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=f20287b7ab8d421e859180a71e519b22gingras@lunenfeld.caMassIVE37MOD:00685 - "A protein modification that effectively converts an L-glutamine residue to L-glutamic acid."MOD:00684 - "A protein modification that effectively converts an L-asparagine residue to L-aspartic acid."MOD:00719 - "A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues."ProteomicsMultiomicsLTQ Orbitrap EliteHomo Sapiens (ncbitaxon:9606)LTRIThe 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. Here we report the crystal structure of the LSM domain of LSM14 bound to a highly conserved C-terminal fragment of 4E-T. The 4E-T C-terminus forms a bi-partite motif that wraps around the N-terminal LSM domain of LSM14. We also determined the crystal structure of LSM14 bound to the C-terminal RecA-like domain of DDX6. LSM14 binds DDX6 via a unique non-contiguous motif with distinct directionality as compared to other DDX6-interacting proteins. Together with mutational and proteomic studies, the LSM14-DDX6 structure reveals that LSM14 has adopted a divergent mode of binding DDX6 in order to support the formation of mRNA silencing complexes and P-body assembly.Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.Brandmann Tobias T, Fakim Hana H, Padamsi Zoya Z, Youn Ji-Young JY, Gingras Anne-Claude AC, Fabian Marc R MR, Jinek Martin M0PXD008505trueBrandmann_LSM14This set of submissions contains the mass spectrometry files for the manuscript by Tobias Brandmann et al. that describes structure function study of LSM14. Affinity-purification experiments were performed using HeLa cells expressing LSM14A wild-type and mutant constructs, and MS files were acquired on Orbitrap Elite. Tue Dec 19 13:29:00 GMT 2017MSV00008183029510985