DFT-MD and vibrational anharmonicities of a phosphorylated amino acid. Success and failure

2010 ◽  
Vol 12 (14) ◽  
pp. 3501 ◽  
Author(s):  
Alvaro Cimas ◽  
Marie-Pierre Gaigeot
Keyword(s):  
Amino Acid ◽  
Phosphorylated Amino Acid

scholarly journals Phosphorylation in vivo of non-ribosomal proteins from native 40 S ribosomal particles of Krebs II mouse ascites-tumour cells

1981 ◽  
Vol 194 (3) ◽  
pp. 1007-1009 ◽  
Author(s):  
J Schuck ◽  
G Reichert ◽  
O G Issinger
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Ribosomal Proteins ◽  
Ribosomal Subunits ◽  
Phosphorylated Amino Acid ◽  
Mouse Ascites ◽  
Independent Protein ◽  
Ascites Tumour Cells

Four non-ribosomal proteins from native 40 S ribosomal subunits with mol.wts. of 110 000, 84 000, 68 000 and 26 000 were phosphorylated in vivo when ascites cells were incubated in the presence of [32P]Pi. The 110 000-, 84 000- and 26 000-dalton proteins are identical with phosphorylated products from native 40 S subunits after phosphorylation in vitro by a cyclic nucleotide-independent protein kinase. Phosphoserine was the major phosphorylated amino acid of the proteins phosphorylated in vivo and in vitro.

Strengths of Hydrogen Bonds Involving Phosphorylated Amino Acid Side Chains

2007 ◽  
Vol 129 (4) ◽  
pp. 820-827 ◽  
Author(s):  
Daniel J. Mandell ◽  
Ilya Chorny ◽  
Eli S. Groban ◽  
Sergio E. Wong ◽  
Elisheva Levine ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Side Chains ◽  
Phosphorylated Amino Acid ◽  
Amino Acid Side Chains

Synthesis and Monolayer Characterization of Phosphorylated Amino Acid Analogs

2002 ◽  
Vol 254 (2) ◽  
pp. 322-330 ◽  
Author(s):  
Johan Ekeroth ◽  
Annika Borgh ◽  
Peter Konradsson ◽  
Bo Liedberg
Keyword(s):  
Amino Acid ◽  
Phosphorylated Amino Acid ◽  
Amino Acid Analogs

scholarly journals Phosphoproteomic identification of vasopressin V2 receptor-dependent signaling in the renal collecting duct

2019 ◽  
Vol 317 (4) ◽  
pp. F789-F804 ◽  
Author(s):  
Venkatesh Deshpande ◽  
Anika Kao ◽  
Viswanathan Raghuram ◽  
Arnab Datta ◽  
Chung-Lin Chou ◽  
...  
Keyword(s):  
Amino Acid ◽  
Collecting Duct ◽  
Water Channel ◽  
Protein Mass ◽  
Web Resource ◽  
Phosphorylated Amino Acid ◽  
Vasopressin V2 Receptor ◽  
Duct Cells ◽  
V2 Receptor ◽  
Collecting Duct Cells

Vasopressin controls water balance largely through PKA-dependent effects to regulate the collecting duct water channel aquaporin-2 (AQP2). Although considerable information has accrued regarding the regulation of water and solute transport in collecting duct cells, information is sparse regarding the signaling connections between PKA and transport responses. Here, we exploited recent advancements in protein mass spectrometry to perform a comprehensive, multiple-replicate analysis of changes in the phosphoproteome of native rat inner medullary collecting duct cells in response to the vasopressin V2 receptor-selective agonist 1-desamino-8D-arginine vasopressin. Of the 10,738 phosphopeptides quantified, only 156 phosphopeptides were significantly increased in abundance, and only 63 phosphopeptides were decreased, indicative of a highly selective response to vasopressin. The list of upregulated phosphosites showed several general characteristics: 1) a preponderance of sites with basic (positively charged) amino acids arginine (R) and lysine (K) in position −2 and −3 relative to the phosphorylated amino acid, consistent with phosphorylation by PKA and/or other basophilic kinases; 2) a greater-than-random likelihood of sites previously demonstrated to be phosphorylated by PKA; 3) a preponderance of sites in membrane proteins, consistent with regulation by membrane association; and 4) a greater-than-random likelihood of sites in proteins with class I COOH-terminal PDZ ligand motifs. The list of downregulated phosphosites showed a preponderance of those with proline in position +1 relative to the phosphorylated amino acid, consistent with either downregulation of proline-directed kinases (e.g., MAPKs or cyclin-dependent kinases) or upregulation of one or more protein phosphatases that selectively dephosphorylate such sites (e.g., protein phosphatase 2A). The phosphoproteomic data were used to create a web resource for the investigation of G protein-coupled receptor signaling and regulation of AQP2-mediated water transport.

Identification of Phosphorylated Amino Acid Residues During Gas Phase Sequencing

1987 ◽  
pp. 479-482
Author(s):  
Yuhuan Wang ◽  
Alexander W. Bell ◽  
Mark A. Hermodson ◽  
Peter J. Roach
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Amino Acid Residues ◽  
Phosphorylated Amino Acid

scholarly journals Nestin Protein Is Phosphorylated in Adult Neural Stem/Progenitor Cells and Not Endothelial Progenitor Cells

2012 ◽  
Vol 2012 ◽  
pp. 1-5 ◽  
Author(s):  
Jun Namiki ◽  
Sayuri Suzuki ◽  
Takeshi Masuda ◽  
Yasushi Ishihama ◽  
Hideyuki Okano
Keyword(s):  
Stem Cells ◽  
Endothelial Cells ◽  
Amino Acid ◽  
Progenitor Cells ◽  
Endothelial Progenitor Cells ◽  
Phosphorylation Sites ◽  
Amino Acid Residues ◽  
Nestin Expression ◽  
Endothelial Progenitor ◽  
Phosphorylated Amino Acid

An intermediate filament protein, Nestin, is known as a neural stem/progenitor cell marker. It was shown to be required for the survival and self-renewal of neural stem cells according to the phenotypes of Nestin knockout mice. Nestin expression has also been reported in vascular endothelial cells, and we recently reported Nestin expression in proliferating endothelial progenitor cells, but not in mature endothelial cells. Using quantitative phosphoproteome analysis, we studied differences in phosphorylation levels between CNS Nestin in adult neural stem cells and vascular Nestin in adult bone-marrow-derived endothelial progenitor cells. We detected 495 phosphopeptides in the cell lysates of adult CNS stem/progenitor cells and identified 11 significant phosphorylated amino acid residues in the Nestin protein. In contrast, endothelial progenitor cells showed no significant phosphorylation of Nestin. We also measured neoplastic endothelial cells of the mouse brain and identified 13 phosphorylated amino acid residues in the Nestin protein. Among the 11 phosphorylated amino acids of adult CNS Nestin, five (S565, S570, S819, S883, and S886) were CNS Nestin-specific phosphorylation sites. Detection of the CNS-specific phosphorylation sites in Nestin, for example, by a phospho-specific Nestin antibody, may allow the expression of CNS Nestin to be distinguished from vascular Nestin.

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