Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1074/jbc.M116.759373 http://scihub22266oqcxt.onion/10.1074/jbc.M116.759373 C5339772!5339772!28154193     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28154193&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 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\28154193.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2017 ; 292 (9): 3919-28 Nephropedia Template TP {{tp|p=28154193|t=2017. Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated ?-Synuclein-selective Autophagic Degradation* |pdf=|usr=}}{{28154193}} gab.com Text Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated -Synuclein-selective Autophagic Degradation* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28154193 #FOAvip Increasing lines of evidence support the causal link between ?-synuclein (?-syn) accumulation in the brain and Parkinson's disease (PD) pathogenesis. Therefore, lowering ?-syn protein levels may represent a viable therapeutic strategy for the treatment of PD and related disorders. We recently described a novel selective ?-syn degradation pathway, catalyzed by the activity of the Polo-like kinase 2 (PLK2), capable of reducing ?-syn protein expression and suppressing its toxicity in vivo. However, the exact molecular mechanisms underlying this degradation route remain elusive. In the present study we report that among PLK family members, PLK3 is also able to catalyze ?-syn phosphorylation and degradation in living cells. Using pharmacological and genetic approaches, we confirmed the implication of the macroautophagy on PLK2-mediated ?-syn turnover, and our observations suggest a concomitant co-degradation of these two proteins. Moreover, we showed that the N-terminal region of ?-syn is important for PLK2-mediated ?-syn phosphorylation and degradation and is implicated in the physical interaction between the two proteins. We also demonstrated that PLK2 polyubiquitination is important for PLK2�?-syn protein complex degradation, and we hypothesize that this post-translational modification may act as a signal for the selective recognition by the macroautophagy machinery. Finally, we observed that the PD-linked mutation E46K enhances PLK2-mediated ?-syn degradation, suggesting that this mutated form is a bona fide substrate of this degradation pathway. In conclusion, our study provides a detailed description of the new degradation route of ?-syn and offers new opportunities for the development of therapeutic strategies aiming to reduce ?-syn protein accumulation and toxicity. Twit Text FOAVip Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated -Synuclein-selective Autophagic Degradation* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28154193 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28154193 #FOAvip English Wikipedia <ref>{{Cite pmid|28154193}}</ref> Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated ?-Synuclein-selective Autophagic Degradation* #MMPMID28154193 Dahmene M; B�rard M; Oueslati A J Biol Chem 2017[Mar]; 292 (9): 3919-28 PMID28154193show ga Increasing lines of evidence support the causal link between ?-synuclein (?-syn) accumulation in the brain and Parkinson's disease (PD) pathogenesis. Therefore, lowering ?-syn protein levels may represent a viable therapeutic strategy for the treatment of PD and related disorders. We recently described a novel selective ?-syn degradation pathway, catalyzed by the activity of the Polo-like kinase 2 (PLK2), capable of reducing ?-syn protein expression and suppressing its toxicity in vivo. However, the exact molecular mechanisms underlying this degradation route remain elusive. In the present study we report that among PLK family members, PLK3 is also able to catalyze ?-syn phosphorylation and degradation in living cells. Using pharmacological and genetic approaches, we confirmed the implication of the macroautophagy on PLK2-mediated ?-syn turnover, and our observations suggest a concomitant co-degradation of these two proteins. Moreover, we showed that the N-terminal region of ?-syn is important for PLK2-mediated ?-syn phosphorylation and degradation and is implicated in the physical interaction between the two proteins. We also demonstrated that PLK2 polyubiquitination is important for PLK2�?-syn protein complex degradation, and we hypothesize that this post-translational modification may act as a signal for the selective recognition by the macroautophagy machinery. Finally, we observed that the PD-linked mutation E46K enhances PLK2-mediated ?-syn degradation, suggesting that this mutated form is a bona fide substrate of this degradation pathway. In conclusion, our study provides a detailed description of the new degradation route of ?-syn and offers new opportunities for the development of therapeutic strategies aiming to reduce ?-syn protein accumulation and toxicity. �Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated ?-Sy(epmc).pdf DeepDyve Pubget Overpricing