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Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multi-site polarity substrate Lgl

2024-09-26

Abstract excerpt

The mutually antagonistic kinase-substrate relationship between the apical aPKC-Par6 heterodimer and the basolateral substrate Lgl is key to the establishment and maintenance of cell polarity across metazoa. Although aPKC-Par6 can phosphorylate Lgl at three serine sites to exclude it from the apical domain, paradoxically, aPKC-Par6 and Lgl can also form a stable kinase-substrate complex whose function remains uncl...

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Literature Corpus work
fdcb9b0d-0c6d-5b04-b654-544a265062e1
DOI
10.1101/2024.09.26.615224
Open publication

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Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multi-site polarity substrate LglDOI 10.1101/2024.09.26.615224
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