About: Research Resource: Identification of Novel Growth Hormone-Regulated Phosphorylation Sites by Quantitative Phosphoproteomics

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About: Research Resource: Identification of Novel Growth Hormone-Regulated Phosphorylation Sites by Quantitative Phosphoproteomics Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Research Resource: Identification of Novel Growth Hormone-Regulated Phosphorylation Sites by Quantitative Phosphoproteomics
Creator	Carter-Su, Christin Andrews, Philip Argetsinger, Lawrence Fingar, Diane Kweon, Hye Ray, Bridgette
Source	PMC
abstract	GH and GH receptors are expressed throughout life, and GH elicits a diverse range of responses, including growth and altered metabolism. It is therefore important to understand the full spectrum of GH signaling pathways and cellular responses. We applied mass spectrometry-based phosphoproteomics combined with stable isotope labeling with amino acids in cell culture to identify proteins rapidly phosphorylated in response to GH in 3T3-F442A preadipocytes. We identified 132 phosphosites in 95 proteins that exhibited rapid (5 or 15 min) GH-dependent statistically significant increases in phosphorylation by more than or equal to 50% and 96 phosphosites in 46 proteins that were down-regulated by GH by more than or equal to 30%. Several of the GH-stimulated phosphorylation sites were known (e.g. regulatory Thr/Tyr in Erks 1 and 2, Tyr in signal transducers and activators of transcription (Stat) 5a and 5b, Ser939 in tuberous sclerosis protein (TSC) 2 or tuberin). The remaining 126 GH-stimulated sites were not previously associated with GH. Kyoto Encyclopedia of Genes and Genomes pathway analysis of GH-stimulated sites indicated enrichment in proteins associated with the insulin and mammalian target of rapamycin (mTOR) pathways, regulation of the actin cytoskeleton, and focal adhesions. Akt/protein kinase A consensus sites (RXRXXS/T) were the most commonly phosphorylated consensus sites. Immunoblotting confirmed GH-stimulated phosphorylation of all seven novel GH-dependent sites tested [regulatory sites in proline-rich Akt substrate, 40 kDA (PRAS40), regulatory associated protein of mTOR, ATP-citrate lyase, Na(+)/H(+) exchanger-1, N-myc downstream regulated gene 1, and Shc]). The immunoblot results suggest that many, if not most, of the GH-stimulated phosphosites identified in this large-scale quantitative phosphoproteomics analysis, including sites in multiple proteins in the Akt/ mTOR complex 1 pathway, are phosphorylated in response to GH. Their identification significantly broadens our thinking of GH-regulated cell functions.
has issue date	2012-05-08(xsd:dateTime)
bibo:doi	10.1210/me.2011-1258
bibo:pmid	22570334
has license	cc-by-nc
sha1sum (hex)	d7ba62869caeb82ebe0dd98756082590d55c68fb
schema:url	https://doi.org/10.1210/me.2011-1258
resource representing a document's title	Research Resource: Identification of Novel Growth Hormone-Regulated Phosphorylation Sites by Quantitative Phosphoproteomics
has PubMed Central identifier	PMC3858665
has PubMed identifier	22570334
schema:publication	Mol Endocrinol
resource representing a document's body	covid:d7ba62869caeb82ebe0dd98756082590d55c68fb#body_text
is schema:about of	named entity 'IDENTIFICATION' named entity 'TUBERIN' named entity 'CELL FUNCTIONS' named entity 'OUR' named entity 'IDENTIFIED' named entity 'STABLE ISOTOPE LABELING WITH AMINO ACIDS IN CELL CULTURE' named entity 'AKT' named entity '3T3-F442A' named entity 'TRANSCRIPTION' named entity 'CELLULAR' named entity 'THINKING' named entity 'THEIR' named entity 'PHOSPHORYLATION' named entity 'INDICATED' named entity 'RESPONSES' named entity 'QUANTITATIVE' named entity 'DIVERSE' named entity 'ACTIN CYTOSKELETON' named entity 'STATISTICALLY SIGNIFICANT' named entity 'INCLUDING' named entity 'PATHWAYS' named entity 'REMAINING' named entity 'ENRICHMENT' named entity 'MASS SPECTROMETRY' named entity 'PHOSPHOPROTEOMICS' named entity 'SUGGEST' named entity 'PHOSPHORYLATION SITES' named entity 'RECEPTORS' named entity 'INSULIN' named entity 'IMPORTANT' named entity 'METABOLISM' named entity 'GROWTH HORMONE' named entity 'PHOSPHORYLATION SITES' named entity 'RESEARCH RESOURCE' named entity 'NOVEL' named entity 'STIMULATED' named entity 'ANALYSIS' named entity 'CONFIRMED' named entity '132' named entity 'PROLINE-RICH AKT SUBSTRATE' named entity 'KINASE' named entity 'BASED' named entity 'QUANTITATIVE' named entity 'REGULATORY ASSOCIATED PROTEIN OF MTOR' named entity 'KDA' named entity 'TRANSDUCERS' named entity '50%' named entity '1056' named entity 'IMMUNOBLOTTING' named entity 'SHC' named entity 'FULL SPECTRUM' named entity 'UNDERSTAND' named entity 'KYOTO ENCYCLOPEDIA OF GENES AND GENOMES' named entity 'MIN' named entity 'REGULATED' named entity 'EXCHANGER' named entity 'PATHWAY' named entity 'TYR' named entity 'INCREASES' named entity 'KNOWN' named entity 'LARGE' named entity 'NOVEL' named entity '126' named entity 'SIGNAL' named entity 'RANGE' named entity 'IMMUNOBLOT' named entity 'DEPENDENT' named entity 'REGULATION' named entity 'PATHWAY ANALYSIS' named entity 'FOCAL ADHESIONS' named entity 'ALTERED' named entity 'SIGNALING PATHWAYS' named entity 'ASSOCIATED WITH' named entity 'RAPID' named entity 'REGULATED' named entity 'RESULTS'

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