{"database":"MassIVE","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://massive-ftp.ucsd.edu/v01/MSV000081830/"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":0,"searchCount":0},"additional":{"submitter":["Anne-Claude Gingras"],"full_dataset_link":["https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=f20287b7ab8d421e859180a71e519b22"],"submitter_email":["gingras@lunenfeld.ca"],"sample_protocol":[""],"repository":["MassIVE"],"file_size":["37"],"ptm_modification":["MOD: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.\""],"data_protocol":[""],"omics_type":["Proteomics","Multiomics"],"instrument_platform":["LTQ Orbitrap Elite"],"species":["Homo Sapiens (ncbitaxon:9606)"],"submitter_affiliation":["LTRI"],"pubmed_abstract":["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. 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."],"pubmed_title":["Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes."],"pubmed_authors":["Brandmann Tobias T, Fakim Hana H, Padamsi Zoya Z, Youn Ji-Young JY, Gingras Anne-Claude AC, Fabian Marc R MR, Jinek Martin M"],"citation_count":["0"],"additional_accession":["PXD008505"]},"is_claimable":true,"name":"Brandmann_LSM14","description":"This 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.  ","dates":{"publication":"Tue Dec 19 13:29:00 GMT 2017"},"accession":"MSV000081830","cross_references":{"pubmed":["29510985"]}}