The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42

@article{Joberty2000TheCP,
  title={The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42},
  author={Gérard Joberty and Clark D Petersen and Lin Gao and Ian G. Macara},
  journal={Nature Cell Biology},
  year={2000},
  volume={2},
  pages={531-539}
}
PAR (partitioning-defective) proteins, which were first identified in the nematode Caenorhabditis elegans, are essential for asymmetric cell division and polarized growth, whereas Cdc42 mediates establishment of cell polarity. Here we describe an unexpected link between these two systems. We have identified a family of mammalian Par6 proteins that are similar to the C. elegans PDZ-domain protein PAR-6. Par6 forms a complex with Cdc42–GTP, with a human homologue of the multi-PDZ protein PAR-3… 
Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C
Asymmetric cell division in the Caenorhabditis elegans embryos requires products of par (partitioning defective) genes 1–6 and atypical protein kinase C (aPKC), whereas Cdc42 and Rac, members of the
Functional cross-talk between Cdc42 and two downstream targets, Par6B and PAK4.
TLDR
It is shown that PAK4 phosphorylates Par6B at Ser143 blocking its interaction with Cdc42, which provides a potential new mechanism for controlling the subcellular localization of Par 6B and its interacting with other proteins.
Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
TLDR
It is shown that depletion of Par-3 in mammalian epithelial cells profoundly disrupts tight junction assembly, and a novel mechanism through which Par- 3 engages in the spatial regulation of Rac activity and establishment of epithelial polarity is revealed.
A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl
TLDR
The data provide a direct physical and regulatory link between proteins of distinct polarity complexes, identify Mlgl as a functional substrate for aP KC in cell polarization and indicate that aPKC is directed to cell polarity substrates through a network of protein–protein interactions.
Cell Polarity 1
  • K. Ebnet
  • Biology
    Springer International Publishing
  • 2015
TLDR
What the authors know about the mechanisms of how the aPKC-PAR complex is specifically positioned and activated and regulates overall cell polarity of epithelial cells is described with special attention to its molecular nature.
The cell polarity protein ASIP/PAR‐3 directly associates with junctional adhesion molecule (JAM)
TLDR
It is suggested that the ASIP/PAR‐3–aPKC complex is tethered to tight junctions via its association with JAM, indicating a potential role for JAM in the generation of cell polarity in epithelial cells.
Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
TLDR
The identification of a biochemical and functional link between these two complexes that is mediated by Par6 and PALS1 is highlighted, highlighting a previously unrecognized link between protein complexes that are essential for epithelial polarity and formation of tight junctions.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 40 REFERENCES
Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans.
TLDR
It is reported that an atypical protein kinase C (PKC-3) is essential for proper asymmetric cell divisions and co-localizes with PAR-3 and concludes that PKC-3 plays an indispensable role in establishing embryonic polarity through interaction withPAR-3.
PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos.
TLDR
The co-dependence of PAR-3, PAR-6 and PKC-3 for peripheral localization and the overlap in their distributions lead us to propose that they act in a protein complex.
An Atypical PKC Directly Associates and Colocalizes at the Epithelial Tight Junction with ASIP, a Mammalian Homologue of Caenorhabditis elegans Polarity Protein PAR-3
TLDR
A role for a protein complex containing ASIP and aPKC in the establishment and/or maintenance of epithelial cell polarity is suggested and its asymmetric distribution in polarized cells from worm embryo to mammalian-differentiated cells may mean that the complex functions generally in the organization of cellular asymmetry.
Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK
TLDR
The solution structure of the complex of Cdc42 with the GTPase-binding domain of ACK is reported, where both proteins undergo significant conformational changes on binding, to form a new type of G-protein/effector complex.
Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor.
TLDR
A cDNA encoding a protein which interacts with the GTP- bound form, but not with the GDP-bound form, of the Rho family members, including RhoA, Racl, and Cdc42, is isolated by the yeast two-hybrid method.
Structure of Cdc42 in complex with the GTPase-binding domain of the ‘Wiskott–Aldrich syndrome’ protein
TLDR
Structural and biochemical data suggest that GBD-sequence divergence outside the CRIB motif may reflect additional regulatory interactions with functional domains that are specific to individual effectors.
Cdc42: An Essential Rho-Type GTPase Controlling Eukaryotic Cell Polarity
TLDR
In the budding yeast Saccharomyces cerevisiae, Cdc42p plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth.
A Conserved Binding Motif Defines Numerous Candidate Target Proteins for Both Cdc42 and Rac GTPases (*)
TLDR
Results indicate that proteins containing the CRIB motif bind to Cdc42 and/or Rac in a GTP-dependent manner, and they may, therefore, participate in downstream signaling.
Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
TLDR
Cdc42 plays a critical part in epithelial-cell polarity, by, unexpectedly, regulating the fidelity of membrane transport in both the endocytic and the secretory pathways.
The Caenorhabditis elegans p21-activated Kinase (CePAK) Colocalizes with CeRac1 and CDC42Ce at Hypodermal Cell Boundaries during Embryo Elongation*
TLDR
Investigation of cDNA coding for the p21-activated kinase homologue (CePAK) in Caenorhabditis elegans development indicates that CePAK is specifically expressed at the hypodermal cell boundaries during embryonic body elongation, which involves dramatic cytoskeletal reorganization.
...
1
2
3
4
...