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10.15252/embr.202052141 http://scihub22266oqcxt.onion/10.15252/embr.202052141 33764618!8097337!33764618     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 269.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+Rep 2021 ; 22 (5): e52141 Nephropedia Template TP {{tp|p=33764618|t=2021. PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates |pdf=|usr=}}{{33764618}} gab.com Text PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates JO: EMBO Rep http://www.kidney.de/pget.php?&tw=1&pmid=33764618 #FOAvip Tyrosine phosphorylation of secretion machinery proteins is a crucial regulatory mechanism for exocytosis. However, the participation of protein tyrosine phosphatases (PTPs) in different exocytosis stages has not been defined. Here we demonstrate that PTP-MEG2 controls multiple steps of catecholamine secretion. Biochemical and crystallographic analyses reveal key residues that govern the interaction between PTP-MEG2 and its substrate, a peptide containing the phosphorylated NSF-pY(83) site, specify PTP-MEG2 substrate selectivity, and modulate the fusion of catecholamine-containing vesicles. Unexpectedly, delineation of PTP-MEG2 mutants along with the NSF binding interface reveals that PTP-MEG2 controls the fusion pore opening through NSF independent mechanisms. Utilizing bioinformatics search and biochemical and electrochemical screening approaches, we uncover that PTP-MEG2 regulates the opening and extension of the fusion pore by dephosphorylating the DYNAMIN2-pY(125) and MUNC18-1-pY(145) sites. Further structural and biochemical analyses confirmed the interaction of PTP-MEG2 with MUNC18-1-pY(145) or DYNAMIN2-pY(125) through a distinct structural basis compared with that of the NSF-pY(83) site. Our studies thus provide mechanistic insights in complex exocytosis processes. Twit Text FOAVip PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates ????EMBO Rep http://www.kidney.de/pget.php?&tw=1&pmid=33764618 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33764618 #FOAvip English Wikipedia <ref>{{Cite pmid|33764618}}</ref> PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates #MMPMID33764618 Xu YF; Chen X; Yang Z; Xiao P; Liu CH; Li KS; Yang XZ; Wang YJ; Zhu ZL; Xu ZG; Zhang S; Wang C; Song YC; Zhao WD; Wang CH; Ji ZL; Zhang ZY; Cui M; Sun JP; Yu X EMBO Rep 2021[May]; 22 (5): e52141 PMID33764618show ga Tyrosine phosphorylation of secretion machinery proteins is a crucial regulatory mechanism for exocytosis. However, the participation of protein tyrosine phosphatases (PTPs) in different exocytosis stages has not been defined. Here we demonstrate that PTP-MEG2 controls multiple steps of catecholamine secretion. Biochemical and crystallographic analyses reveal key residues that govern the interaction between PTP-MEG2 and its substrate, a peptide containing the phosphorylated NSF-pY(83) site, specify PTP-MEG2 substrate selectivity, and modulate the fusion of catecholamine-containing vesicles. Unexpectedly, delineation of PTP-MEG2 mutants along with the NSF binding interface reveals that PTP-MEG2 controls the fusion pore opening through NSF independent mechanisms. Utilizing bioinformatics search and biochemical and electrochemical screening approaches, we uncover that PTP-MEG2 regulates the opening and extension of the fusion pore by dephosphorylating the DYNAMIN2-pY(125) and MUNC18-1-pY(145) sites. Further structural and biochemical analyses confirmed the interaction of PTP-MEG2 with MUNC18-1-pY(145) or DYNAMIN2-pY(125) through a distinct structural basis compared with that of the NSF-pY(83) site. Our studies thus provide mechanistic insights in complex exocytosis processes. |*Protein Tyrosine Phosphatases, Non-Receptor/metabolism[MESH] |*Protein Tyrosine Phosphatases/metabolism[MESH] |Peptides[MESH]PTP-MEG2 regulates quantal size and fusion pore opening through two di(epmc).pdf DeepDyve Pubget Overpricing