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10.12688/f1000research.14427.1 http://scihub22266oqcxt.onion/10.12688/f1000research.14427.1 C6020718!6020718 !29983916     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29983916 &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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29983916 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       F1000Res 2018 ; 7 (ä): ä Nephropedia Template TP {{tp|p=29983916 |t=2018. aPKC: the Kinase that Phosphorylates Cell Polarity |pdf=|usr=}}{{29983916 }} gab.com Text aPKC: the Kinase that Phosphorylates Cell Polarity JO: F1000Res http://www.kidney.de/pget.php?&tw=1&pmid=29983916 #FOAvip Establishing and maintaining cell polarity are dynamic processes that necessitate complicated but highly regulated protein interactions. Phosphorylation is a powerful mechanism for cells to control the function and subcellular localization of a target protein, and multiple kinases have played critical roles in cell polarity. Among them, atypical protein kinase C (aPKC) is likely the most studied kinase in cell polarity and has the largest number of downstream substrates characterized so far. More than half of the polarity proteins that are essential for regulating cell polarity have been identified as aPKC substrates. This review covers mainly studies of aPKC in regulating anterior-posterior polarity in the worm one-cell embryo and apical-basal polarity in epithelial cells and asymmetrically dividing cells (for example, Drosophila neuroblasts). We will go through aPKC target proteins in cell polarity and discuss various mechanisms by which aPKC phosphorylation controls their subcellular localizations and biological functions. We will also review the recent progress in determining the detailed molecular mechanisms in spatial and temporal control of aPKC subcellular localization and kinase activity during cell polarization. Twit Text FOAVip aPKC: the Kinase that Phosphorylates Cell Polarity ????F1000Res http://www.kidney.de/pget.php?&tw=1&pmid=29983916 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29983916 #FOAvip English Wikipedia <ref>{{Cite pmid|29983916 }}</ref> aPKC: the Kinase that Phosphorylates Cell Polarity #MMPMID29983916 Hong Y F1000Res 2018[]; 7 (ä): ä PMID29983916 show ga Establishing and maintaining cell polarity are dynamic processes that necessitate complicated but highly regulated protein interactions. Phosphorylation is a powerful mechanism for cells to control the function and subcellular localization of a target protein, and multiple kinases have played critical roles in cell polarity. Among them, atypical protein kinase C (aPKC) is likely the most studied kinase in cell polarity and has the largest number of downstream substrates characterized so far. More than half of the polarity proteins that are essential for regulating cell polarity have been identified as aPKC substrates. This review covers mainly studies of aPKC in regulating anterior-posterior polarity in the worm one-cell embryo and apical-basal polarity in epithelial cells and asymmetrically dividing cells (for example, Drosophila neuroblasts). We will go through aPKC target proteins in cell polarity and discuss various mechanisms by which aPKC phosphorylation controls their subcellular localizations and biological functions. We will also review the recent progress in determining the detailed molecular mechanisms in spatial and temporal control of aPKC subcellular localization and kinase activity during cell polarization. äaPKC: the Kinase that Phosphorylates Cell Polarity (epmc).pdf DeepDyve Pubget Overpricing