KLHL-perheestä: KLHL2 (ABP-KELCH, MAV, MAYVEN, 4q32.)

https://www.ncbi.nlm.nih.gov/gene/11275

Related articles in PubMed

1. Role of Mayven, a kelch-related protein in oligodendrocyte process formation. Williams SK, et al. J Neurosci Res, 2005 Sep 1. PMID 16035103Abstract
   Oligodendrocyte function is central to the maintenance of the normal nervous system in health and disease. In particular, process formation and the generation of large sheets of myelin are important components of their biological properties. We have investigated the role of Mayven, a recently identified member of the kelch family of proteins, in process extension in oligodendrocyte-lineage cells. The kelch superfamily consists of a large number of structurally diverse proteins characterized by the presence of a kelch-repeat domain. Other members of this family associate with the actin cytoskeleton and regulate process length. Mayven is expressed predominantly in the CNS, has six kelch repeats, and is an actin-binding protein, associating with actin through its kelch-repeat domain. We have cloned rat Mayven and examined its role in the oligodendrocyte lineage by using RT-PCR, RNA interference, and a truncated, dominant-negative myc-tagged Mayven. Oligodendrocyte precursors treated with siRNA directed to Mayven have reduced process length, but there was no change in migration or expression of differentiation markers. Immunocytochemistry demonstrated that Mayven associated with F-actin at cell tips. Finally, overexpression of truncated Mayven lacking the SH3 ligand binding domain in oligodendrocyte-lineage cells resulted in shorter process formation, which was augmented when the cells were plated on laminin and fibronectin. These data suggest a role for Mayven in oligodendrocyte precursor cell process formation.
2. Mayven induces c-Jun expression and cyclin D1 activation in breast cancer cells. Bu X, et al.
   Oncogene. 2005 Mar 31;24(14):2398-409.
   Mayven is a member of the kelch-related superfamily of proteins, characterized by a series of 'kelch' repeats at their carboxyl terminus and a BTB/POZ domain at their NH2-terminus. Little is known about the role of Mayven in cancer. Here, we report that Mayven expression was abundant and diffuse in primary human epithelial breast tumor cells as compared to normal breast epithelial cells, where Mayven was detected in the normal breast layer of the mammary ducts. Overexpression of Mayven resulted in an induction of c-Jun protein levels, as well as increased AP-1 (activating protein 1) transcriptional activity in MCF-7 and T47D breast cancer cells through its BTB/POZ domain. Furthermore, Mayven activated c-Jun N-terminal kinase in breast cancer cells. Mayven, through its BTB/POZ domain, induced cyclin D1 expression and cyclin D1 promoter activity and promoted cell cycle progression from the G1 to S phase. MCF-7 cells transduced with the recombinant retroviral sense Mayven (pMIG-W-Mayven) showed significant induction of c-Jun and cyclin D1 mRNA expression and activities as compared to the retroviral vector alone, while MCF-7 cells transduced by the recombinant retroviral antisense Mayven (pMIG-W-Mayven-AS) demonstrated a significant decrease in c-Jun and cyclin D1 expression and activities. Given the crucial functions of cyclin D1 and AP-1 signaling in oncogenesis, our results strongly suggest that overexpression of Mayven may promote tumor growth through c-Jun and cyclin D1.
3. hDKIR, a human homologue of the Drosophila kelch protein, involved in a ring-like structure. Mai A, et al. Exp Cell Res, 2004 Oct 15. PMID 15383316
4. Structural and biochemical characterization of the KLHL3-WNK kinase interaction important in blood pressure regulation. Schumacher FR, et al. Biochem J, 2014 Jun 1. PMID 24641320, Free PMC Article
5. Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain. Soltysik-Espanola M, et al. Mol Biol Cell, 1999 Jul. PMID 10397770, Free PMC Article

See all (29) citations in PubMed
Löydän ZID geenin yhteydessä tämän arftikkeli ZID on ZBTB6, ZNF482(9q33.2) 
https://www.ncbi.nlm.nih.gov/pubmed/19121354/
 We now demonstrate that NAC1 acts as a corepressor for other POZ/BTB proteins. NAC1 is a POZ/BTB motif containing transcriptional repressor protein. In a mammalian two hybrid assay in neuronal (N2A) cells and non-neuronal (HEK 293T) cells, VP16 activation domain tagged NAC1 resulted in significant reversal of transcriptional inhibition with the Gal4-ZID, Gal4-BCL6, Gal4-ZF5, and kelch proteins Gal4-MAYVEN and Gal4-NRP/B fusion proteins. We also observed similar results with another corepressor, BCoR Gal4 fusion protein. NAC1 potentiated ZF5 mediated repression in Gal4-DBD fusion transient assays. GST pulldown assays further confirmed protein-protein interactions between these proteins and NAC1. Both the NAC1 isoforms demonstrated selective interaction through the POZ/BTB domain but not with the non-POZ/BTB region. Endogenous NAC1 and BCL6 physically associated in CNS regions. Strikingly, NAC1 did not interact with the pro-myelocytic leukemia zinc finger protein (PLZF), another POZ/BTB protein that is not found in the adult brain. Therefore, we conclude that NAC1 functions as a corepressor for POZ/BTB proteins expressed in the mature CNS.

Conserved Domains (2) summary

sd00038
Location:490 → 534

Kelch; KELCH repeat [structural motif]. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.

cl28614
Location:60 → 577

BTB; Broad-Complex, Tramtrack and Bric a brac. Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.