{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Peuchen EH"],"funding":["NICHD NIH HHS","NIGMS NIH HHS"],"pagination":["15647"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5688136"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["The earliest stages of animal development are largely controlled by changes in protein phosphorylation mediated by signaling pathways and cyclin-dependent kinases. In order to decipher these complex networks and to discover new aspects of regulation by this post-translational modification, we undertook an analysis of the X. laevis phosphoproteome at seven developmental stages beginning with stage VI oocytes and ending with two-cell embryos. Concurrent measurement of the proteome and phosphoproteome enabled measurement of phosphosite occupancy as a function of developmental stage. We observed little change in protein expression levels during this period. We detected the expected phosphorylation of MAP kinases, translational regulatory proteins, and subunits of APC/C that validate the accuracy of our measurements. We find that more than half the identified proteins possess multiple sites of phosphorylation that are often clustered, where kinases work together in a hierarchical manner to create stretches of phosphorylated residues, which may be a means to amplify signals or stabilize a particular protein conformation. Conversely, other proteins have opposing sites of phosphorylation that seemingly reflect distinct changes in activity during this developmental timeline."],"journal":["Scientific reports"],"pubmed_title":["Phosphorylation Dynamics Dominate the Regulated Proteome during Early Xenopus Development."],"pmcid":["PMC5688136"],"funding_grant_id":["R01 GM096767","R01 HD084399","P41 GM108538"],"pubmed_authors":["Sun L","Champion MM","Dovichi NJ","Huber PW","Peuchen EH","Cox OF","Hebert AS","Coon JJ"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation Dynamics Dominate the Regulated Proteome during Early Xenopus Development.","description":"The earliest stages of animal development are largely controlled by changes in protein phosphorylation mediated by signaling pathways and cyclin-dependent kinases. In order to decipher these complex networks and to discover new aspects of regulation by this post-translational modification, we undertook an analysis of the X. laevis phosphoproteome at seven developmental stages beginning with stage VI oocytes and ending with two-cell embryos. Concurrent measurement of the proteome and phosphoproteome enabled measurement of phosphosite occupancy as a function of developmental stage. We observed little change in protein expression levels during this period. We detected the expected phosphorylation of MAP kinases, translational regulatory proteins, and subunits of APC/C that validate the accuracy of our measurements. We find that more than half the identified proteins possess multiple sites of phosphorylation that are often clustered, where kinases work together in a hierarchical manner to create stretches of phosphorylated residues, which may be a means to amplify signals or stabilize a particular protein conformation. Conversely, other proteins have opposing sites of phosphorylation that seemingly reflect distinct changes in activity during this developmental timeline.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Nov","modification":"2024-11-15T08:40:58.988Z","creation":"2019-03-27T00:08:03Z"},"accession":"S-EPMC5688136","cross_references":{"pubmed":["29142207"],"doi":["10.1038/s41598-017-15936-y"]}}