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10.1073/pnas.1620529114 http://scihub22266oqcxt.onion/10.1073/pnas.1620529114 C5584407!5584407 !28808029     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28808029 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (35 ): E7255-E7261 Nephropedia Template TP {{tp|p=28808029 |t=2017. Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation |pdf=|usr=}}{{28808029 }} gab.com Text Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28808029 #FOAvip Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time. Unraveling this complex PTM code is one of the great challenges in molecular biology. Here, using mass spectrometry-based assays, we focus on the most common PTMs-phosphorylation and O-GlcNAcylation-and investigate how they affect each other. We demonstrate two generic crosstalk mechanisms. First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation. Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates. A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site. Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes. Twit Text FOAVip Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28808029 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28808029 #FOAvip English Wikipedia <ref>{{Cite pmid|28808029 }}</ref> Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation #MMPMID28808029 Leney AC ; El Atmioui D ; Wu W ; Ovaa H ; Heck AJR Proc Natl Acad Sci U S A 2017[Aug]; 114 (35 ): E7255-E7261 PMID28808029 show ga Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time. Unraveling this complex PTM code is one of the great challenges in molecular biology. Here, using mass spectrometry-based assays, we focus on the most common PTMs-phosphorylation and O-GlcNAcylation-and investigate how they affect each other. We demonstrate two generic crosstalk mechanisms. First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation. Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates. A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site. Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes. |Acetylglucosamine/metabolism [MESH] |Amino Acid Motifs/physiology [MESH] |Amino Acid Sequence [MESH] |Glycosylation [MESH] |Humans [MESH] |Mass Spectrometry/methods [MESH] |N-Acetylglucosaminyltransferases/metabolism/physiology [MESH] |Phosphorylation/*physiology [MESH] |Proline [MESH] |Protein Processing, Post-Translational/*physiology [MESH] |Proteins/metabolism [MESH] |Proteolysis [MESH] |Serine [MESH] |Signal Transduction [MESH]Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcy(epmc).pdf DeepDyve Pubget Overpricing