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10.1016/j.cmet.2014.09.013 http://scihub22266oqcxt.onion/10.1016/j.cmet.2014.09.013 C5693325!5693325!25448702     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Metab 2014 ; 20 (6): 939-52 Nephropedia Template TP {{tp|p=25448702|t=2014. AMPK ? sensing energy while talking to other signaling pathways |pdf=|usr=}}{{25448702}} gab.com Text AMPK sensing energy while talking to other signaling pathways JO: Cell Metab http://www.kidney.de/pget.php?&tw=1&pmid=25448702 #FOAvip The AMP-activated protein kinase (AMPK) is a sensor of cellular energy and nutrient status, expressed almost universally in eukaryotes as heterotrimeric complexes comprising catalytic (?) and regulatory (? and ?) subunits. Along with the mechanistic target-of-rapamycin complex-1 (mTORC1), AMPK may have been one of the earliest signaling pathways to have arisen during eukaryotic evolution. Recent crystal structures have provided insights into the mechanisms by which AMPK is regulated by phosphorylation and allosteric activators. Another recent development has been the realization that activation of AMPK by the upstream kinase LKB1 may primarily occur not in the cytoplasm but at the surface of the lysosome, where AMPK and mTORC1 are regulated in a reciprocal manner by the availability of nutrients. It is also becoming clear that there is a substantial amount of crosstalk between the AMPK pathway and other signaling pathways that promote cell growth and proliferation, and this will be discussed. Twit Text FOAVip AMPK sensing energy while talking to other signaling pathways ????Cell Metab http://www.kidney.de/pget.php?&tw=1&pmid=25448702 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25448702 #FOAvip English Wikipedia <ref>{{Cite pmid|25448702}}</ref> AMPK ? sensing energy while talking to other signaling pathways #MMPMID25448702 Hardie DG Cell Metab 2014[Dec]; 20 (6): 939-52 PMID25448702show ga The AMP-activated protein kinase (AMPK) is a sensor of cellular energy and nutrient status, expressed almost universally in eukaryotes as heterotrimeric complexes comprising catalytic (?) and regulatory (? and ?) subunits. Along with the mechanistic target-of-rapamycin complex-1 (mTORC1), AMPK may have been one of the earliest signaling pathways to have arisen during eukaryotic evolution. Recent crystal structures have provided insights into the mechanisms by which AMPK is regulated by phosphorylation and allosteric activators. Another recent development has been the realization that activation of AMPK by the upstream kinase LKB1 may primarily occur not in the cytoplasm but at the surface of the lysosome, where AMPK and mTORC1 are regulated in a reciprocal manner by the availability of nutrients. It is also becoming clear that there is a substantial amount of crosstalk between the AMPK pathway and other signaling pathways that promote cell growth and proliferation, and this will be discussed. äAMPK ? sensing energy while talking to other signaling pathways (epmc).pdf DeepDyve Pubget Overpricing