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Par-6 partitioning defective 6 homolog alpha

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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Cdc42, CAN, Actin, V1a, Rhodopsin
Papers using Par6 antibodies
The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation
Etienne-Manneville Sandrine et al., In The Journal of Cell Biology, 1999
... from Invitrogen, anti-pericentrin from BabCO, anti-GM130, anti-EEA1, and anti-Rac1 from BD, anti-Arf6 from AbCam, anti-Cdc42, anti-Par6, and anti-PKCζ from Santa Cruz Biotechnology, Inc., anti-PKCζ pT410 from ...
Drosophila atypical protein kinase C associates with Bazooka and controls polarity of epithelia and neuroblasts
Ohno Shigeo et al., In The Journal of Cell Biology, 1999
... To obtain cDNA clone(s) covering the entire human PAR-6 protein coding region, we performed backscreening of a human kidney cDNA library (CLONTECH Laboratories, Inc.) using this ...
Papers on Par6
A combined binary interaction and phenotypic map of C. elegans cell polarity proteins.
Boxem et al., Utrecht, Netherlands. In Nat Cell Biol, Feb 2016
We demonstrate the predictive capabilities of the network by showing that the physical interaction between the RhoGAP PAC-1 and PAR-6 is required for radial polarization of the C. elegans embryo.
RasGRF2 controls nuclear migration in postnatal retinal cone photoreceptors.
Santos et al., Salamanca, Spain. In J Cell Sci, Feb 2016
Mechanistically, the generation of this phenotype involved disruption of the outer limiting membrane (OLM), and intrusion into the PS layer, of cone nuclei displaying significant perinuclear accumulation of signaling molecules known to participate in nuclear migration and cytoskeletal reorganization such as PAR3, PAR6, and activated, phosphorylated forms of PAK, MLC2 and VASP.
The aPKC/Par3/Par6 Polarity Complex and Membrane Order Are Functionally Interdependent in Epithelia During Vertebrate Organogenesis.
Gaus et al., Australia. In Traffic, Jan 2016
The differential distribution of lipids between apical and basolateral membranes is necessary for many epithelial cell functions, but how this characteristic membrane organization is integrated within the polarity network during ductal organ development is poorly understood.
Cdc42 regulates epithelial cell polarity and cytoskeletal function during kidney tubule development.
Zent et al., Nashville, United States. In J Cell Sci, Jan 2016
Additionally, in vitro analysis of Cdc42-null collecting duct cells shows that Cdc42 controls these processes by regulating the polarity Par complex (Par3-Par6-aPKC-Cdc42) and the cytoskeletal proteins N-Wasp and ezrin.
Stage-Dependent Axon Transport of Proteasomes Contributes to Axon Development.
Cheng et al., Taipei, Taiwan. In Dev Cell, Dec 2015
Blockade of retrograde transport caused accumulation of proteasomes, reduction of axon growth, and attenuation of growth-associated Par6 at the axon tip of newly polarized neurons.
Dynamic Opposition of Clustered Proteins Stabilizes Cortical Polarity in the C. elegans Zygote.
Munro et al., Chicago, United States. In Dev Cell, Nov 2015
PAR-3 and CDC-42 are both required locally to recruit PAR-6/PKC-3, which inhibits PAR-1 (shown previously) and inhibits local growth/accumulation of CHIN-1 clusters.
Mammalian aPKC/Par polarity complex mediated regulation of epithelial division orientation and cell fate.
Niessen et al., Köln, Germany. In Exp Cell Res, 2014
In this review we will focus on the role of the polarity complex aPKC/Par3/Par6 in the regulation of division orientation and cell fate in different mammalian epithelia.
Single-molecule analysis of cell surface dynamics in Caenorhabditis elegans embryos.
Munro et al., Chicago, United States. In Nat Methods, 2014
We used these methods to (i) resolve distinct mobility states and spatial variation in exchange rates of the polarity protein PAR-6 and (ii) measure spatiotemporal modulation of actin filament assembly and disassembly.
The Par3-like polarity protein Par3L is essential for mammary stem cell maintenance.
Macara et al., Nashville, United States. In Nat Cell Biol, 2014
The Par polarity proteins play key roles in asymmetric division of Drosophila melanogaster stem cells; however, whether the same mechanisms control stem cells in mammals is controversial.
Going vertical: functional role and working principles of the protein Inscuteable in asymmetric cell divisions.
Mapelli et al., Milano, Italy. In Cell Mol Life Sci, 2013
To date, the molecular explanation to account for this phenotype envisioned Insc as an adaptor molecule bridging between the polarity proteins Par3:Par6:aPKC and the spindle pulling machines assembled on NuMA:LGN:Gαi.
The Par3/Par6/aPKC complex and epithelial cell polarity.
Zhang et al., Hong Kong, Hong Kong. In Exp Cell Res, 2013
This review focuses on recent developments of the Par3/Par6/aPKC complex and its interacting proteins in epithelial cell polarity.
Nuclear movement during myotube formation is microtubule and dynein dependent and is regulated by Cdc42, Par6 and Par3.
Gomes et al., Paris, France. In Embo Rep, 2012
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.
On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN.
Gonzalez et al., Milano, Italy. In Open Biol, 2012
The protein network coordinating the spindle position with cortical polarity includes the molecular machinery pulling on astral microtubules, which is assembled on conserved NuMA:LGN:Gαi complexes, the polarity proteins Par3:Par6:aPKC and an adaptor molecule known as Inscuteable (Insc).
Partitioning-defective protein 6 (Par-6) activates atypical protein kinase C (aPKC) by pseudosubstrate displacement.
Prehoda et al., Eugene, United States. In J Biol Chem, 2012
Par-6 allosterically activates aPKC to allow for high spatial and temporal control of substrate phosphorylation and polarization.
Pak6 protein kinase is a novel effector of an atypical Rho family GTPase Chp/RhoV.
Korobko et al., Moscow, Russia. In Biochemistry (mosc), 2012
Pak6 is a binding partner and a outatuve effector protein for the atypical rho GTPase cdc42 homologous protein.
The blood-testis barrier and its implications for male contraception.
Mruk et al., New York City, United States. In Pharmacol Rev, 2012
Studies have demonstrated that some unlikely partners, namely adhesion protein complexes (e.g., occludin-ZO-1, N-cadherin-β-catenin, claudin-5-ZO-1), steroids (e.g., testosterone, estradiol-17β), nonreceptor protein kinases (e.g., focal adhesion kinase, c-Src, c-Yes), polarity proteins (e.g., PAR6, Cdc42, 14-3-3), endocytic vesicle proteins (e.g., clathrin, caveolin, dynamin 2), and actin regulatory proteins (e.g., Eps8, Arp2/3 complex), are working together, apparently under the overall influence of cytokines (e.g., transforming growth factor-β3, tumor necrosis factor-α, interleukin-1α).
The apical polarity protein network in Drosophila epithelial cells: regulation of polarity, junctions, morphogenesis, cell growth, and survival.
Tepass, Toronto, Canada. In Annu Rev Cell Dev Biol, 2011
APRs compose a diverse set of molecules including a transmembrane protein (Crumbs), a serine/threonine kinase (aPKC), a lipid phosphatase (PTEN), a small GTPase (Cdc42), FERM domain proteins (Moesin, Yurt), and several adaptor or scaffolding proteins (Bazooka/Par3, Par6, Stardust, Patj).
A conformational switch in the CRIB-PDZ module of Par-6.
Volkman et al., Milwaukee, United States. In Structure, 2011
a unique dipeptide switch in the Par-6 PDZ domain transmits a signal for allosteric activation to the ligand-binding pocket
aPKC phosphorylates NuMA-related LIN-5 to position the mitotic spindle during asymmetric division.
van den Heuvel et al., Utrecht, Netherlands. In Nat Cell Biol, 2011
In animals, an evolutionarily conserved pathway of LIN-5 (homologues: Mud and NuMA), GPR-1/2 (homologues: Pins, LGN, AGS-3) and Gα mediates spindle positioning, and acts downstream of the conserved PAR-3-PAR-6-aPKC polarity complex.
Par6B and atypical PKC regulate mitotic spindle orientation during epithelial morphogenesis.
Hall et al., New York City, United States. In J Biol Chem, 2011
Data conclude that Par6B and aPKC control mitotic spindle orientation in polarized epithelia and, furthermore, that aPKC coordinately regulates multiple processes to promote morphogenesis.
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