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Lgl1 (show Klra7 Proteins) forms two distinct complexes in vivo, Lgl1 (show Klra7 Proteins)-NMIIA and Lgl1 (show Klra7 Proteins)-Par6alpha-aPKCzeta (show PRKCZ Proteins), and that the formation of these complexes is affected by the phosphorylation state of Lgl1 (show Klra7 Proteins).
Our results provide the first in vivo characterization of RalA (show rala Proteins) 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 (show DCTN1 Proteins) complex, and requires Cdc42 (show CDC42 Proteins), Par6 and Par3 (show F2RL2 Proteins).
PAR6 has a role in forming primordial follicles in mouse ovary
Rin (show RIT2 Proteins) and Rit (show RIT1 Proteins) Bind to PAR6 GTP (show AK3 Proteins)-dependently and regulate cell transformation
Par6alpha-mediated inhibition of insulin (show INS Proteins)-dependent glycogen (show GYS1 Proteins) synthesis in C2C12 cells depends on the direct interaction of Par6alpha with aPKC and on aPKC-mediated T34 phosphorylation of Akt1 (show AKT1 Proteins).
In addition to regulating Par-6-aPKC localization, Cdc42 (show CDC42 Proteins) increases aPKC activity by relieving Par-6 inhibition.
Neph1 (show NEPH1 Proteins)-Nephrin (show NPHS1 Proteins) proteins bind the Par3 (show F2RL2 Proteins)-Par6-atypical protein kinase C (show PRKCZ Proteins) (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 (show TGFB1 Proteins)-Par6 polarity pathway has a role in breast cancer progression
Shp2 (show PTPN11 Proteins) promotes metastasis of prostate cancer by attenuating the PAR3 (show F2RL2 Proteins)/PAR6/aPKC polarity protein complex and enhancing epithelial-to-mesenchymal transition
TGFbeta (show TGFB1 Proteins) 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 (show PRKCZ Proteins). The p-Par6-aPKCzeta (show PRKCZ Proteins) complex is important for cell migration and invasion.
Data indicate that both tumor focality and Par3 (show F2RL2 Proteins)/Par6/atypical protein kinase C (show PRKCZ Proteins) (APKC) expression were significantly associated with tumor recurrence.
BDNF (show BDNF Proteins) can regulate formation of functional synapses by increasing the expression of the RhoA (show RHOA Proteins) inhibitors, Par6C and Rnd3 (show RND3 Proteins).
Morg1 (show wdr83 Proteins) facilitates Par6-aPKC binding to Crb3 (show CRB3 Proteins) 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 (show PRKCZ Proteins) kinase activity, as well as an association with PAR6, were found to be important for PAR6 phosphorylation.
Pak6 (show PAK6 Proteins) is a binding partner and a outatuve effector protein for the atypical rho GTPase (show RACGAP1 Proteins) cdc42 (show CDC42 Proteins) homologous protein.
Data show that DDR1 (show DDR1 Proteins) coordinates the Par3 (show F2RL2 Proteins)/Par6 cell-polarity complex through its carboxy terminus, binding PDZ domains in Par3 (show F2RL2 Proteins) and Par6.
Par6alpha controls centrosome organization through its association with the dynactin (show DCTN1 Proteins) subunit p150(Glued (show DCTN1 Proteins)).
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 (show CSTB Proteins)-2.1/2/CDK-1 (show CDK1 Proteins) antagonize CUL-2 (show CUL2 Proteins) 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 (show CDH1 Proteins), 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 (show AFG3L2 Proteins) polarity arises from coupling of advective transport by flowing cell cortex to a multistable PAR (show AFG3L2 Proteins) 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 (show F2RL1 Proteins) and PAR-6, which localize to opposing PAR (show AFG3L2 Proteins) 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 (show AFG3L2 Proteins) 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 (show CDC42 Proteins)-dependent binding site and PAR-3-mediated release of this inhibition provide a key mechanism for the anterior accumulation of PAR-6.
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