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PDZ domain containing 1

PDZK1, PDZ domain-containing protein
This gene encodes a PDZ domain-containing scaffolding protein. PDZ domain-containing molecules bind to and mediate the subcellular localization of target proteins. The encoded protein mediates the localization of cell surface proteins and plays a critical role in cholesterol metabolism by regulating the HDL receptor, scavenger receptor class B type 1. Single nucleotide polymorphisms in this gene may be associated with metabolic syndrome, and overexpression of this gene may play a role in drug resistance of multiple myeloma. Pseudogenes of this gene are located on the long arm of chromosome 1. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: V1a, CAN, ACID, HDL, CD36
Papers using PDZK1 antibodies
Differential regulation of the renal sodium-phosphate cotransporters NaPi-IIa, NaPi-IIc, and PiT-2 in dietary potassium deficiency
Levi Moshe et al., In American Journal of Physiology - Renal Physiology, 2000
... The PDZK1 (CLAMP1) antibody was from BD Biosciences (San Jose, CA) and ...
Papers on PDZK1
CAPG and GIPC1: Breast Cancer Biomarkers for Bone Metastasis Development and Treatment.
Brown et al., Leeds, United Kingdom. In J Natl Cancer Inst, Apr 2016
RESULTS: Two novel biomarker candidates, macrophage-capping protein (CAPG) and PDZ domain-containing protein GIPC1 (GIPC1), were identified for clinical validation.
Ouabain Regulates CFTR-Mediated Anion Secretion and Na,K-ATPase Transport in ADPKD Cells.
Blanco et al., Kansas City, United States. In J Membr Biol, Dec 2015
Ouabain increased the trafficking of CFTR to the plasma membrane and up-regulated the expression of the CFTR activator PDZK1.
MAGI3 negatively regulates Wnt/β-catenin signaling and suppresses malignant phenotypes of glioma cells.
He et al., Beijing, China. In Oncotarget, Dec 2015
Here, we showed that the PDZ domain-containing protein membrane-associated guanylate kinase inverted 3 (MAGI3) was downregulated at the both mRNA and protein levels in human glioma samples.
Prostacyclin receptors: Transcriptional regulation and novel signalling mechanisms.
Kinsella et al., Dublin, Ireland. In Prostaglandins Other Lipid Mediat, Sep 2015
Moreover, the functional implications of the interactions between the IP with PDZK1, a multi PDZ-domain containing protein essential for reverse-cholesterol transport and endothelialization, and the IP with IKEPP, the intestinal and kidney enriched PDZ protein, for the role of the prostacyclin-IP axis within the vasculature are reviewed.
HDL signaling and protection against coronary artery atherosclerosis in mice.
Fuller et al., Hamilton, Canada. In J Biomed Res, Sep 2015
These signaling responses require the HDL receptor, scavenger receptor class B type 1 (SR-B1), an adaptor protein (PDZK1) that binds to the cytosolic C terminus of SR-B1, Akt1 activation and (at least in endothelial cells) activation of endothelial NO synthase (eNOS).
Genome-wide association analysis of more than 120,000 individuals identifies 15 new susceptibility loci for breast cancer.
Easton et al., Brisbane, Australia. In Nat Genet, Apr 2015
Combining association analysis with ChIP-seq chromatin binding data in mammary cell lines and ChIA-PET chromatin interaction data from ENCODE, we identified likely target genes in two regions: SETBP1 at 18q12.3 and RNF115 and PDZK1 at 1q21.1.
An update on the genetic architecture of hyperuricemia and gout.
Merriman, Dunedin, New Zealand. In Arthritis Res Ther, 2014
At the other 26 loci, probable causal genes can be identified at three (PDZK1, SLC22A11, and INHBB) with strong candidates at a further 10 loci.
Genetic polymorphisms in the PDZK1 gene and susceptibility to gout in male Han Chinese: a case-control study.
Zhang et al., Harbin, China. In Int J Clin Exp Med, 2014
PDZK1 acts as a scaffolding protein for a large variety of transporter and regulatory proteins, and has been identified in the kidney.
Beyond cell-cell adhesion: Emerging roles of the tight junction scaffold ZO-2.
Bauer et al., Salzburg, Austria. In Tissue Barriers, 2013
Recent evidence suggests that ZO-2 is also involved in stress response and cytoprotective mechanisms, which further highlights the multi-faceted nature of this PDZ domain-containing protein.
The PDZ protein discs-large (DLG): the 'Jekyll and Hyde' of the epithelial polarity proteins.
Marsh et al., Birmingham, United Kingdom. In Febs J, 2012
Discs-large (DLG) is a multi-PDZ domain-containing protein that belongs to the family of molecular scaffolding proteins known as membrane guanylate kinases or MAGUKs.
[Importance of the hyperuricaemia, gout and gender nosological features in the activity of general practitioner - family doctor].
Rudichenko, In Lik Sprava, 2012
Several genes are known for their influence on serum uric acid: PDZK1, GCKR, SLC2A9, ABCG2, LRRC16A, SLC17A3, SLC16A9 and SLC22A12.
PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-β3 (PLC-β3)-specific activation of somatostatin by forming a ternary complex with PLC-β3 and somatostatin receptors.
Suh et al., South Korea. In J Biol Chem, 2012
PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-beta3 (PLC-beta3)-specific activation of somatostatin by forming a ternary complex with PLC-beta3 and somatostatin receptors.
PDZK1 regulates breast cancer resistance protein in small intestine.
Kato et al., Kanazawa, Japan. In Drug Metab Dispos, 2011
PDZK1 plays a pivotal role in the apical localization of BCRP.
Interaction of the human prostacyclin receptor with the PDZ adapter protein PDZK1: role in endothelial cell migration and angiogenesis.
Kinsella et al., Dublin, Ireland. In Mol Biol Cell, 2011
Human prostacyclin receptor interacts with the PDZ adapter protein PDZK1; this interaction plays important role in endothelial cell migration and angiogenesis.
Identification of the PDZ3 domain of the adaptor protein PDZK1 as a second, physiologically functional binding site for the C terminus of the high density lipoprotein receptor scavenger receptor class B type I.
Krieger et al., Boston, United States. In J Biol Chem, 2011
PDZK1-mediated control of hepatic SR-BI requires direct binding of the SR-BI C terminus to either the PDZ1 or PDZ3 domains, and that binding to both domains simultaneously is not required for PDZK1 control of hepatic SR-BI.
Role of PDZK1 protein in apical membrane expression of renal sodium-coupled phosphate transporters.
Levi et al., Aurora, United States. In J Biol Chem, 2011
The differential affinity of the Na/P(i) transporters for NHERF-1 and PDZK1 proteins could partially explain their differential regulation and/or stability in the apical membrane.
Relationship between plasma estradiol levels and estrogen-responsive gene expression in estrogen receptor-positive breast cancer in postmenopausal women.
Dowsett et al., London, United Kingdom. In J Clin Oncol, 2010
Results The expression of many known estrogen-responsive genes and gene sets was highly significantly associated with plasma E2 levels (eg, TFF1/pS2, GREB1, PDZK1 and PGR; P < .005).
Spatiotemporal coupling of cAMP transporter to CFTR chloride channel function in the gut epithelia.
Naren et al., Memphis, United States. In Cell, 2007
CFTR single-channel recordings and FRET-based intracellular cAMP dynamics suggest that a compartmentalized coupling of cAMP transporter and CFTR occurs via the PDZ scaffolding protein, PDZK1, forming a macromolecular complex at apical surfaces of gut epithelia.
A defect in harmonin, a PDZ domain-containing protein expressed in the inner ear sensory hair cells, underlies Usher syndrome type 1C.
Petit et al., Paris, France. In Nat Genet, 2000
We identified this gene (USH1C), encoding a PDZ-domain-containing protein, harmonin, in a subtracted mouse cDNA library derived from inner ear sensory areas.
GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors.
Huganir et al., Baltimore, United States. In Nature, 1997
Here we identify a synaptic PDZ domain-containing protein GRIP (glutamate receptor interacting protein) that specifically interacts with the C termini of AMPA receptors.
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