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Lgl1 forms two distinct complexes in vivo, Lgl1-NMIIA and Lgl1-Par6alpha-aPKCzeta, and that the formation of these complexes is affected by the phosphorylation state of Lgl1.
Our results provide the first in vivo characterization of RalA function in the mammalian brain and highlight a novel
The nucleus of a myoblast moves rapidly after fusion towards the central myotube nuclei which is driven by microtubules and dynein/dynactin complex, and requires Cdc42, Par6 and Par3.
PAR6 has a role in forming primordial follicles in mouse ovary
During neuronal migration the centrosome acts to coordinate cytoskeletal dynamics in response to mPar6alpha-mediated signaling.
Rin and Rit Bind to PAR6 GTP-dependently and regulate cell transformation
Par6alpha-mediated inhibition of insulin-dependent glycogen synthesis in C2C12 cells depends on the direct interaction of Par6alpha with aPKC and on aPKC-mediated T34 phosphorylation of Akt1.
In addition to regulating Par-6-aPKC localization, Cdc42 increases aPKC activity by relieving Par-6 inhibition.
Neph1-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity
The aPKC-PAR3 complex associates with the nephrin-podocin complex in podocytes through direct interaction between PAR3 and nephrin, and the kinase activity of aPKC is required for the appropriate distribution of nephrin and podocin in podocytes.
the TGFbeta-Par6 polarity pathway has a role in breast cancer progression
In T84 cells, overexpression of Par-6 causes intestinal barrier dysfunction. Lipopolysaccharide (LPS)-induced intestinal epithelial barrier dysfunction and increase in Par-6 expression was prevented by AhR activation.
Studies indicate that the PAR3-PAR6-aPKC complex are important for the establishment of neuronal polarity [Review].
We first demonstrate that Hook2 is essential for the polarized Golgi re-orientation towards the migration front. Depletion of Hook2 results in a decrease of PAR6alpha at the centrosome during cell migration, while overexpression of Hook2 in cells induced the formation of aggresomes with the recruitment of PAR6alpha, aPKC and PAR3
Roles of partitioning-defective protein 6 (Par6) and its complexes in the proliferation, migration and invasion of cancer cells
Shp2 promotes metastasis of prostate cancer by attenuating the PAR3/PAR6/aPKC polarity protein complex and enhancing epithelial-to-mesenchymal transition
TGFbeta induced Par6 phosphorylation on Ser345 and its recruitment to the leading edge of the membrane ruffle in migrating PC-3U cells, where it colocalised with aPKCzeta. The p-Par6-aPKCzeta complex is important for cell migration and invasion.
Data indicate that both tumor focality and Par3/Par6/atypical protein kinase C (APKC) expression were significantly associated with tumor recurrence.
BDNF can regulate formation of functional synapses by increasing the expression of the RhoA inhibitors, Par6C and Rnd3.
Morg1 facilitates Par6-aPKC binding to Crb3 for definition of apical identity of epithelial cells.
Par6 negatively regulates trophoblast fusion via its roles on tight junctions and cytoskeleton dynamics and provide novel insight into the contribution of this polarity marker in altered trophoblast cell fusion typical of preeclampsia.
Atypical protein kinase C kinase activity, as well as an association with PAR6, were found to be important for PAR6 phosphorylation.
Pak6 is a binding partner and a outatuve effector protein for the atypical rho GTPase cdc42 homologous protein.
Data show that DDR1 coordinates the Par3/Par6 cell-polarity complex through its carboxy terminus, binding PDZ domains in Par3 and Par6.
Par6alpha controls centrosome organization through its association with the dynactin subunit p150(Glued).
Partitioning-defective protein 6 associated constitutively with endogenous aPKCs.
crystal structure of the complex of PKCiota and Par6alpha PB1 domains to a resolution of 1.5 A
A rare A/G polymorphism in the promoter of the Par6alpha gene is associated with reduced fasting glycaemia, increased glucose tolerance and reduced serum nonesterified fatty Acids concentrations.
findings demonstrated that G-protein-activated phospholipase C-beta interacts with cell polarity proteins Par3 and Par6 to form protein complexes and to mediate downstream signal transduction
Studies in this review confirm that signaling by Par6alpha controls the migration of immature granule neurons down the Bergmann glial fibers into the internal granule cell layer in which they establish synaptic connections.
We provide evidence for the existence of a distinct PAR protein complex in endothelial cells. Both PAR-3 and PAR-6 associate directly with the adherens junction protein vascular endothelial cadherin (VE-cadherin).
we find that vab-1 lies in the same genetic pathway as cdc-42 and is responsible for polarizing CDC-42 activity to the medial tip. Together, these data establish a previously uncharacterized role for polarized CDC-42, in conjunction with PAR-6, PAR-3 and an Eph receptor(vab-1), during epithelial intercalation.
Our results support a model in which CYB-2.1/2/CDK-1 antagonize CUL-2 activity to promote stabilization of PAR-6 levels during polarization of the early C. elegans embryo.
the arcade cell epithelium polarizes by a PAR-6-mediated pathway that is independent of E-cadherin, beta-integrin and beta-laminin.
PAR-3 and PAR-6 function in cytokinesis may be partially redundant and play a role in the maintenance of DYN-1 in the cleavage furrow.
evidence PAR polarity arises from coupling of advective transport by flowing cell cortex to a multistable PAR reaction-diffusion system; advection in active, flowing medium provides mechanism for mechanically templated pattern formation in development
Centrosomes localize apically by first moving toward lateral foci of the conserved polarity proteins PAR-3 and PAR-6, then move together with these foci toward the future apical surface. Embryos lacking PAR-3 fail to localize their centrosomes apically.
PAR-2 and PAR-6, which localize to opposing PAR domains, undergo exchange between well mixed cytoplasmic populations and laterally diffusing membrane-associated states
Binding to PKC-3, but not to PAR-3 or to a conventional PDZ domain ligand, is required for PAR-6 function in C. elegans
PAR proteins function in both apicobasal and anterior-posterior asymmetry during the first few cell cycles of embryogenesis.
CDC-37-mediated inhibition of the CDC-42-dependent binding site and PAR-3-mediated release of this inhibition provide a key mechanism for the anterior accumulation of PAR-6.
CDC-42 interaction with PAR-6 is not required for the initial establishment of asymmetry but is required for maximal cortical accumulation of PAR-6 and to maintain its asymmetry.
PAR-6 is required for junction formation but not apicobasal polarization in C. elegans embryonic epithelial cells.
nos-3 loss of function mutant suppresses the lethality of par-2 mutants by regulating PAR-6 protein levels.
study identified a RhoGAP, PAC-1, which mediates embryo radial polarity & gastrulation by excluding PAR-6 from contacted cell surfaces; PAC-1 provides a dynamic molecular link between cell contacts & PAR proteins that polarizes embryos radially
This gene is a member of the PAR6 family and encodes a protein with a PSD95/Discs-large/ZO1 (PDZ) domain and a semi-Cdc42/Rac interactive binding (CRIB) domain. This cell membrane protein is involved in asymmetrical cell division and cell polarization processes as a member of a multi-protein complex. The protein also has a role in the epithelial-to-mesenchymal transition (EMT) that characterizes the invasive phenotype associated with metastatic carcinomas. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
par-6 partitioning defective 6 homolog alpha (C. elegans)
, partitioning defective 6 homolog alpha
, PAR-6 alpha
, Tax interaction protein 40
, partitioning defective protein 6A
, Tax-interacting protein 40
, par-6 partitioning defective 6 homolog alpha
, partitioning defective-6 homolog alpha
, partitioning-defective protein 6
, tax interaction protein 40