The PAR proteins: fundamental players in animal cell polarization.

By B. Goldstein, I. Macara. Developmental Cell, 2007

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View Paper: https://www.semanticscholar.org/paper/2ea3efb5ce8e4239d47051f1bb8d8b26b6c7d5c4

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Citations in the corpus

Life at the leading edge. (2011, background): “The Par complex, in turn, is known to be important for assembly of cell-cell junctions and is often regulated by Cdc42 (Goldstein and Macara, 2007).”
Transcriptional regulation of cell polarity in EMT and cancer (2008, background): “The PAR complex is localized to the apical junction domain, and significant evidence indicates that it has an important function in the assembly of tight junctions (reviewed by Goldstein and Macara, 2007; Ebnet, 2008).”
From cells to organs: building polarized tissue (2008, background): “Cell polarity involves the asymmetric organization of most of the physical aspects of the cell, including the cell surface, intracellular organelles and the cytoskeleto”
Tight junctions at the blood brain barrier: physiological architecture and disease-associated dysregulation (2012, positive): “The participation of this PCP complex to TJ integrity was further illustrated by the recent observation that meningococcal adhesion to human cerebral endothelial cells recruited Par-3, Par-6 and aPKC-ζ under bacterial colonies and induced disruption of cell-cell junctions [156].”
Mechanisms of asymmetric stem cell division. (2008, background): “Before mitosis, the proteins Par-3, Par-6, atypical PKC (aPKC), Inscuteable, Pins, Gai, and Mud (see below for their individual functions) accumulate on the apical side of the cell cortex (Betschinger and Knoblich, 2004; Suzuki and Ohno, 2006; Goldstein and Macara, 2007).”
A molecular network for de novo generation of the apical surface and lumen (2010, background): “Annexin2–Cdc42 associates with Rab11a-positive vesicles during lumenogenesis Luminal targeting of aPKC in MDCK cysts requires interaction of GTP–Cdc42 with the phosphatidylinositol (4,5)-bisphosphate-binding protein, Annexin2 (Anx2)6.”
Mammalian Rho GTPases: new insights into their functions from in vivo studies (2008, background): “CDC42 seems to function primarily through the polarity protein partitioning-defective-6 (PAR6) and thereby with PAR3 and/or atypical protein kinase C (aPKC) isoforms to induce polarity in several different animal model”
Mechanical control of tissue and organ development (2010, background): “This local enrichment of myosin II is established by the recruitment of PAR proteins (PAR-3 and PAR-6) to the free apical membrane (Goldstein and Macara, 2007; Nance et al., 2003), much as asymmetry is established in the egg and in earlier embryonic tissues, as described above.”