The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl

By J. Betschinger, K. Mechtler, Juergen A. Knoblich. Nature, 2003

616 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/465fc5f550c45bafeec76d1bb330bb329a27c9a2

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In Cell Biology

Citations in the corpus

Mechanisms of asymmetric stem cell division. (2008, background): “Lgl is phosphorylated by aPKC on three conserved serines in a region that separates the N-terminal b-propellers and the less conserved C-terminal region of the protein (Betschinger et al., 2003).”
Tight junctions and cell polarity. (2006, background): “Studies show that aPKC directly interacts with and phosphorylates Lgl and that this phosphorylation event regulates the localization of Lgl, controlling polarity in Drosophila and mammalian cells (Betschinger et al. 2003, Plant et al. 2003, Yamanaka et al. 2003).”
Asymmetric self-renewal and commitment of satellite stem cells in muscle. (2007, background): “Within the stem cell niche, signaling pathways such as Wnt, Notch, BMP/TGFb, and STAT and proteins such as Numb, PAR, PKCz, LGL, and NUMA have been implicated in the regulation of asymmetric cell division in model systems (Betschinger and Knoblich, 2004; Betschinger et al., 2003; Fuchs et al., 2004;”
Renal defects associated with improper polarization of the CRB and DLG polarity complexes in MALS-3 knockout mice (2007, positive): “This PAR-3 complex excludes certain basolateral proteins from the apical domain via aPKC phosphorylation (Betschinger et al., 2003; Plant et al., 2003).”
Cdc42 - the centre of polarity (2004, background): “The Par6aPKC complex also interacts with the tumour suppressor Lethal giant larvae (Lgl), with aPKC phosphorylating it at highly conserved residues (Betschinger et al., 2003).”