KCTD1( 18q11.12) säätelee negatiivisesti AP-2 ja Wnt -signalointia . Interaktio prioniproteiinin PrPC kanssa.

 KCTD1 (18q11.12),  
 https://www.ncbi.nlm.nih.gov/gene/284252
Tämä kaliumkanava-tetramerisatiodomeenin 1 sisältävä proteiini säätelee negatiivisesti AP-2 transkriptiopreotiiniperhettä ja Wnt-signalointia. Se  edistää beta-kateniinin ubikitinaatiota ja degradaatiota. Jos tämä- geeni mutatoituu, ilmenee SEN-oireyhtymä scalp-ear-nipple-syndrome.  geeni ezpressoituu ihossa ja ruokatorvessa  ja 21 muussa kudoksessa. Tämnä proteiini aggrekoituu Cu jonivaikutuksesta ja  tekee  filamentteja.  PrP(C) prioniproteiini tekee interaktion KCTD1:n kanssa.  Zn/ Cu jonisuhteella on merkitys.

KCTD1

Official Full Name

potassium channel tetramerization domain containing 1provided by HGNC

Also known as

C18orf5

Summary

This gene encodes a protein containing a BTB (Broad-complex, tramtrack and bric a brac), also known as a POZ (POXvirus and zinc finger) protein-protein interaction domain. The encoded protein negatively regulates the AP-2 family of transcription factors and the Wnt signaling pathway. A mechanism for the modulation of Wnt signaling has been proposed in which the encoded protein enhances ubiquitination and degradation of the beta-catenin protein. Mutations in this gene have been identified in Scalp-ear-nipple (SEN) syndrome. [provided by RefSeq, May 2017]

Expression

Broad expression in skin (RPKM 10.7), esophagus (RPKM 8.1) , brain, and 20 other tissues See more

Preferred Names

BTB/POZ domain-containing protein KCTD1

Related articles in PubMed

1. Bivalent Copper Ions Promote Fibrillar Aggregation of KCTD1 and Induce Cytotoxicity. Liu Z, et al. Sci Rep, 2016 Sep 6. PMID 27596723, Free PMC Article
2. Sci Rep. 2016 Sep 6;6:32658. doi: 10.1038/srep32658.
   Bivalent Copper Ions Promote Fibrillar Aggregation of KCTD1 and Induce Cytotoxicity.
   
   Liu Z¹, Song F¹, Ma ZL¹, Xiong Q¹, Wang J¹, Guo D¹, Sun G¹.
   School of Basic Medical Sciences, Wuhan University, Wuhan 430072, P.R. China.
   Abstract
   

   Potassium channel tetramerization domain containing 1 (KCTD1) family members have a BTB/POZ domain, which can facilitate protein-protein interactions involved in the regulation of different signaling pathways. KCTD proteins have potential Zn(2+)/Cu(2+) binding sites with currently unknown structural and functional roles. We investigated potential Cu(2+)-specific effects on KCTD1 using circular dichroism, turbidity measurement, fluorescent dye binding, proteinase K (PK) digestion, cell proliferation and apoptosis assays. These experiments indicate that the KCTD1 secondary structure assumes greater β-sheet content and the proteins aggregate into a PK-resistant form under 20 μM Cu(2+), and this β-sheet-rich aggregation with Cu(2+) promotes fibril formation, which results in increased cell toxicity by apoptosis. Our results reveal a novel role for Cu(2+) in determining the structure and function of KCTD1.

   PMID:

   27596723

   PMCID:

   PMC5011690

   DOI:

   10.1038/srep32658

   [Indexed for MEDLINE]

   Free PMC Article
3. 
   
4.  
5. Mutations in KCTD1 cause scalp-ear-nipple syndrome. Marneros AG, et al. Am J Hum Genet, 2013 Apr 4. PMID 23541344, Free PMC Article
6. Expression, purification, and secondary structure characterization of recombinant KCTD1. Mei F, et al. Biochemistry (Mosc), 2012 Aug. PMID 22860917
7. Crypton transposons: identification of new diverse families and ancient domestication events. Kojima KK, et al. Mob DNA, 2011 Oct 19. PMID 22011512, Free PMC Article
8. KCTD1 suppresses canonical Wnt signaling pathway by enhancing β-catenin degradation. Li X, et al. PLoS One, 2014. PMID 24736394, Free PMC Article
9.  https://www.ncbi.nlm.nih.gov/pubmed/22138399  
   To identify molecular interaction partners of the cellular prion protein (PrP(C)), we applied a yeast two-hybrid screen on a bovine brain cDNA expression library and identified the potassium channel tetramerization domain containing 1 (KCTD1) as a PrP(C) interacting protein. Deletion mapping showed that PrP(C) specifically binds KCTD1 through the unstructured PrP(51-136) region. We further confirmed the interaction between PrP(C) and KCDT1 protein by co-immunoprecipitation in vivo and by a biosensor assay in vitro. Interestingly, the binding of an insertion mutant PrP(8OR) to KCTD1 is higher than that of wild-type PrP(C), suggesting an important role for an unstructured region harboring octapeptide repeats in the KCTD1-PrP(C) interaction. Our results identify a novel PrP(C)-interacting protein and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C).
   

   Copyright © 2011 Elsevier Inc. All rights reserved.

   
   

   DOI:

   10.1016/j.bbrc.2011.11.081
   RED,  PrCP and Cu2+: 
   

   The plasma zinc/serum Cu2+ ratio as a biomarker in children with autism spectrum disorders

   Article in Biomarkers 14(3):171-80 · April 2009 with 253 Reads 
   

   DOI: 10.1080/13547500902783747 · Source: PubMed  
   

   The frequency of zinc deficiency, copper toxicity and low zinc/copper in children with autism spectrum disorders (ASDs) may indicate decrement in metallothionein system functioning. A retrospective review of plasma zinc, serum copper and zinc/copper was performed on data from 230 children with autistic disorder, pervasive developmental disorder-NOS and Asperger’s syndrome. The entire cohort’s mean zinc level was 77.2 μg dl⁻¹, mean copper level was 131.5 μg dl⁻¹, and mean Zn/Cu was 0.608, which was below the 0.7 cut-off of the lowest 2.5% of healthy children. The plasma zinc/serum copper ratio may be a biomarker of heavy metal, particularly mercury, toxicity in children with ASDs.

   Keywords: Plasma zinc/serum copper ratio, zinc deficiency, metallothionein system dysfunction, mercury, autistic disorder, pervasive developmental disorder-NOS, Asperger’s syndrome 

See all (23) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

1. results reveal a novel role for Cu(2+) in determining the structure and function of KCTD1
2. The authors find that the KCTD proteins 5, 6, 9 and 17 bind to Cul3 with high affinity, while the KCTD proteins 1 and 16 do not have detectable binding.
3. KCTD1 functions as a novel inhibitor of Wnt signaling p
4. Mutations in KCTD1 cause scalp-ear-nipple syndrome.
5. Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
6. indicate the novel function of KCTD1 as the transcriptional repressor for AP-2 family, especially for AP-2alpha

KUPARI Copper
https://www.ncbi.nlm.nih.gov/books/NBK225400/