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Par-3 plays an important role in the modulation of intestinal barrier function by regulating delivery of occludin as well as suppression of MLC phosphorylation.
HTT (show HTT Proteins) is required for the apical localization of PAR3 (show F2RL2 Proteins)-aPKC during epithelial morphogenesis in virgin, pregnant, and lactating mice.
Authors identify the cell polarity protein Par3, a negative regulator of neuronal differentiation, as a Smek1 (show SMEK1 Proteins) substrate and demonstrate that Smek1 (show SMEK1 Proteins) suppresses its activity.
Par3 (show F2RL2 Proteins) (and protein kinase C zeta (show PRKCZ Proteins)) are activated in neurons when binding to N2-proteoglygan.
Suggest that loss of Par3 (show F2RL2 Proteins) promotes metastatic behaviour of ErbB2 (show ERBB2 Proteins)-induced breast tumour epithelial cells by decreasing cell-cell cohesion.
Par3 (show F2RL2 Proteins) is identified as a regulator of signaling pathways relevant to invasive breast cancer.
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 (show PARD6A Proteins) and Par3 (show F2RL2 Proteins).
Data suggest that aPKC phosphorylates JAM-A (show F11R Proteins) at S285 to regulate cell-cell contact maturation, TJ formation, and single lumen specification.
Brain-derived neurotrophic factor (BDNF (show BDNF Proteins)) induces polarized signaling of small GTPase (show RACGAP1 Proteins) (Rac1) protein at the onset of Schwann cell myelination through partitioning-defective 3 (Par3 (show F2RL2 Proteins)) protein.
Report a willin(FRMD6 (show FRMD6 Proteins))/Par3 (show F2RL2 Proteins)-aPKC-ROCK pathway that controls epithelial apical morphology.
Studies suggest that rare deleterious variants of PARD3 in the aPKC-binding region contribute to human cranial neural tube defect (NTD).
These data highlight the importance of the carboxy-terminal motif of the E6 protein and downregulation of PAR3 (show F2RL2 Proteins) in tumorigenic transformation of human cervical keratinocytes.
Results suggest that Par3 (show F2RL2 Proteins) expression is likely involved in ovarian cancer progression, especially in peritoneal metastasis, probably through modulating IL-6 (show IL6 Proteins) /STAT3 (show STAT3 Proteins) signaling.
reduced keratinocytes Par3 function fosters a permissive P-cadherin-dependent niche for melanocytes transformation, invasion, and metastasis.
These results demonstrate the importance of Par3 (show F2RL2 Proteins) and SNAIL (show SNAI1 Proteins) in development of KSHV-induced B-cells cancers
PAR-3 (show F2RL2 Proteins) protein expression is frequently lost in primary esophageal squamous cell carcinoma and loss of the PAR-3 (show F2RL2 Proteins) protein is associated with aggressive clinicopathological features.
Taken together, these results suggest that the Par3 (show F2RL2 Proteins) regulates invasion and metastasis in pancreatic cancers by controlling tight junction assembly via Tiam1 (show TIAM1 Proteins).
Knockdown of the polarity protein Par3 reversed the effects of Galpha13 (show GNA13 Proteins) knockdown on cell-cell adhesion and proteolytic invasion in three-dimensional collagen.
Shp2 (show PTPN11 Proteins) promotes metastasis of prostate cancer by attenuating the PAR3 (show F2RL2 Proteins)/PAR6 (show PARD6A Proteins)/aPKC polarity protein complex and enhancing epithelial-to-mesenchymal transition
Pard3 mediates contact inhibition between neural crest cells and promotes timely myelin gene expression but is not essential for neural crest migration or myelination.
these results demonstrate a novel role of Par3 during neural crest migration, which is likely to be conserved in other processes that involve contact inhibition of locomotion such as cancer invasion or cell dispersion.
Pard3 and Rab11a (show RAB11A Proteins) are necessary for lumen formation in the neural rod.
Brain-derived neurotrophic factor (BDNF (show BDNF Proteins)) induces polarized signaling of small GTPase (show RACGAP1 Proteins) (Rac1) protein at the onset of Schwann cell myelination through partitioning-defective 3 (Par3) protein.
Study demonstrates that the microtubule cytoskeleton gradually transitions from a radial to linear organization during neurulation and that microtubules function in conjunction with the polarity protein Pard3 to mediate centrosome positioning.
Agouti signaling (ASIP) genes exist in many species in lower vertebrates and were most probably present in early stages of vertebrate evolution.
Apical localization of ASIP in neuroepithelial cells involves the oligomerization domain CR1, the PDZ domains, and the C-terminal portion of the protein.
This gene encodes a member of the PARD protein family. PARD family members interact with other PARD family members and other proteins\; they affect asymmetrical cell division and direct polarized cell growth. Multiple alternatively spliced transcript variants have been described for this gene.
partitioning-defective protein 3 homolog
, partitioning defective 3 homolog
, par-3 partitioning defective 3 homolog (C. elegans)
, atypical PKC isotype-specific-interacting protein
, ephrin-interacting protein
, atypical PKC-specific binding protein
, atypical PKC-specific-binding protein
, partitioning-defective 3 homolog
, three-PDZ containing protein similar to C. elegans PAR3 (partitioning defect)
, CTCL tumor antigen se2-5
, atypical PKC isotype-specific interacting protein
, par-3 family cell polarity regulator alpha
, par-3 partitioning defective 3 homolog