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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Kelch-like 12

KLHL12, Kelch-like 12
Top mentioned proteins: Cul3, Ubiquitin, Cullin, RP42, PKI
Papers on KLHL12
The Pathway of Collagen Secretion.
Erlmann et al., In Annu Rev Cell Dev Biol, Dec 2015
Cullin3, an E3 ligase, and its specific adaptor protein, KLHL12, ubiquitinate Sec31, which could increase the size of COPII coats.
Anti-kelch-like 12 and anti-hexokinase 1: novel autoantibodies in primary biliary cirrhosis.
Gershwin et al., San Diego, United States. In Liver Int, Feb 2015
BACKGROUND & AIMS: Using high-density human recombinant protein microarrays, we identified two potential biomarkers, kelch-like 12 (KLHL12) and hexokinase-1 (HK1), in primary biliary cirrhosis (PBC).
KLHL12 Promotes Non-Lysine Ubiquitination of the Dopamine Receptors D4.2 and D4.4, but Not of the ADHD-Associated D4.7 Variant.
Van Craenenbroeck et al., Gent, Belgium. In Plos One, 2014
KLHL12 PROMOTES UBIQUITINATION OF THE DOPAMINE D4 RECEPTOR ON NON-LYSINE RESIDUES: In previous studies we have shown that KLHL12, a BTB-Kelch protein, specifically interacts with the polymorphic repeats of the dopamine D4 receptor and enhances its ubiquitination, which, however, has no influence on receptor degradation.
A regulator of secretory vesicle size, Kelch-like protein 12, facilitates the secretion of apolipoprotein B100 and very-low-density lipoproteins--brief report.
Fisher et al., Montréal, Canada. In Arterioscler Thromb Vasc Biol, 2014
APPROACH AND RESULTS: Expression levels of Kelch-like protein 12 (KLHL12), an adaptor protein known to assist COPII-dependent transport of procollagen, were manipulated by using a KLHL12-specific small interfering RNA and a KLHL12 expression plasmid in the rat hepatoma cell line, McArdle RH7777.
Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases.
Bullock et al., Oxford, United Kingdom. In J Biol Chem, 2013
To define the molecular basis for this assembly and the overall architecture of the E3, we determined the crystal structures of the BTB-BACK domains of KLHL11 both alone and in complex with Cul3, along with the Kelch domain structures of KLHL2 (Mayven), KLHL7, KLHL12, and KBTBD5.
Ubiquitin-dependent regulation of COPII coat size and function.
Rape et al., Berkeley, United States. In Nature, 2012
Here, we identified the ubiquitin ligase CUL3-KLHL12 as a regulator of COPII coat formation.
Nucleoredoxin sustains Wnt/β-catenin signaling by retaining a pool of inactive dishevelled protein.
Miki et al., Suita, Japan. In Curr Biol, 2010
Kelch-like 12 (KLHL12) targets Dvl for ubiquitination and degradation, suggesting its potential importance in avoiding aberrant Dvl overexpression.
KLHL12-mediated ubiquitination of the dopamine D4 receptor does not target the receptor for degradation.
Van Craenenbroeck et al., Gent, Belgium. In Cell Signal, 2010
In previous studies, we identified KLHL12 as a novel interaction partner of the dopamine D4 receptor that functions as an adaptor in a Cullin3-based E3 ubiquitin ligase complex to target the receptor for ubiquitination.
BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase.
Van Craenenbroeck et al., Gent, Belgium. In J Biol Chem, 2008
KLHL12 specifically interacts with the D4 polymorphism, thereby building up a Cul3-E3 ligase complex with substrate specificity toward the D4 receptor
The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation.
Moon et al., Seattle, United States. In Nat Cell Biol, 2006
Using a tandem-affinity purification strategy and mass spectrometry we have identified proteins associated with Dishevelled, including a Cullin-3 ubiquitin ligase complex containing the Broad Complex, Tramtrack and Bric à Brac (BTB) protein Kelch-like 12 (KLHL12).
Identification of specific autoantigens in Sjögren's syndrome by SEREX.
Kozaki et al., Nagoya, Japan. In Immunology, 2005
IFI16 and two kelch-like proteins, KLHL12 and KLHL7, were found to be novel autoantigens in SjS by SEREX.
hDKIR, a human homologue of the Drosophila kelch protein, involved in a ring-like structure.
Yonehara et al., Saga, Japan. In Exp Cell Res, 2004
molecular cloning and characterization of a novel gene, encoded a human kelch protein containing 568 amino acid residues, termed hDKIR.
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