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10.1016/j.tibs.2015.01.001 http://scihub22266oqcxt.onion/10.1016/j.tibs.2015.01.001 C4340714!4340714!25665457     free     free     free       Trends+Biochem+Sci 2015 ; 40 (3): 149-56 Nephropedia Template TP {{tp|p=25665457|t=2015. Regulation of Mammalian Ste20 (Mst) kinases |pdf=|usr=}}{{25665457}} gab.com Text Regulation of Mammalian Ste20 (Mst) kinases JO: Trends Biochem Sci http://www.kidney.de/pget.php?&tw=1&pmid=25665457 #FOAvip Initially identified as mammalian homologs to yeast Ste20 kinases, the Mst1/2 kinases have been widely investigated subsequent to their rediscovery as key components of the Hippo tumor suppressor pathway in flies. To date, our understanding of Mst substrates and downstream signaling outstrips our knowledge of how these enzymes are controlled by upstream signals. While much remains to be discovered regarding the mechanisms of Mst regulation, it is clear that Mst1 kinase activity is governed at least in part by its state of dimerization, including self-association and also heterodimerization with a variety of other signaling partners. Here, we review the basic architecture of Mst signaling and function and discuss recent advances in our understanding of how these important kinases are regulated. Twit Text FOAVip Regulation of Mammalian Ste20 (Mst) kinases ????Trends Biochem Sci http://www.kidney.de/pget.php?&tw=1&pmid=25665457 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25665457 #FOAvip English Wikipedia <ref>{{Cite pmid|25665457}}</ref> Regulation of Mammalian Ste20 (Mst) kinases #MMPMID25665457 Rawat SJ; Chernoff J Trends Biochem Sci 2015[Mar]; 40 (3): 149-56 PMID25665457show ga Initially identified as mammalian homologs to yeast Ste20 kinases, the Mst1/2 kinases have been widely investigated subsequent to their rediscovery as key components of the Hippo tumor suppressor pathway in flies. To date, our understanding of Mst substrates and downstream signaling outstrips our knowledge of how these enzymes are controlled by upstream signals. While much remains to be discovered regarding the mechanisms of Mst regulation, it is clear that Mst1 kinase activity is governed at least in part by its state of dimerization, including self-association and also heterodimerization with a variety of other signaling partners. Here, we review the basic architecture of Mst signaling and function and discuss recent advances in our understanding of how these important kinases are regulated. äRegulation of Mammalian Ste20 (Mst) kinases (epmc).pdf DeepDyve Pubget Overpricing