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PXD017133

PXD017133 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleIdentification of cGAS post-translational modifications
DescriptionDNA derived from the genetic material of pathogens or from cellular DNA damage provides a molecular pattern that can be sensed by pattern-recognition receptors of the mammalian innate immune system. In recent years, the cyclic GMP-AMP synthase (cGAS) protein has been characterized as a primary cytosolic DNA sensor during infection with bacteria, DNA viruses, or retroviruses. While the role of cGAS in downstream immune signaling through STING-TBK1-IRF3 proteins is well-defined, regulatory mechanisms of cGAS activity, such as through post-translational modifications (PTMs), are still an active area of research. Here, we report a comprehensive characterization of cGAS phosphorylations and acetylations in multiple cell types, HEK293T, primary human fibroblast, and THP-1 cells. A total of 11 PTMs (4 phosphorylations and 7 acetylations) were validated through a combination of data-dependent proteomic analysis and parallel reaction monitoring targeted MS on immunoaffinity purified cGAS. Of these, 3 phosphorylations and 5 acetylations have not been previously identified. The functions of these modifications were investigated by generating a series of mutants and measuring cGAS-dependent apoptotic and immune signaling activities.
HostingRepositoryPanoramaPublic
AnnounceDate2020-05-08
AnnouncementXMLSubmission_2020-05-08_13:57:03.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterTodd Greco
SpeciesList scientific name: Homo sapiens; NCBI TaxID: 9606;
ModificationListPhospho; Acetyl; Carbamidomethyl
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-01-15 23:35:19ID requested
12020-05-08 13:57:05announced
Publication List
Song B, Greco TM, Lum KK, Taber C, Cristea IM, The DNA sensor cGAS is decorated by acetylation and phosphorylation modifications in the context of immune signaling. Mol Cell Proteomics, ():(2020) [pubmed]
Keyword List
submitter keyword: phosphorylation, acetylation, immune response, herpesvirus, IP-MS
Contact List
Ileana Cristea
contact affiliationPrinceton University
contact emailicristea@princeton.edu
lab head
Todd Greco
contact affiliationPrinceton University
contact emailtgreco@princeton.edu
dataset submitter
Full Dataset Link List
Panorama Public dataset URI