KLHL17(1p36.33) , aktiinifiliini, aivospesifinen F-aktiinia sitova Kelch- proteiini

Summary

The protein encoded by this gene is expressed in neurons of most regions of the brain. It contains an N-terminal BTB domain, which mediates dimerization of the protein, and a C-terminal Kelch domain, which mediates binding to F-actin. This protein may play a key role in the regulation of actin-based neuronal function. [provided by RefSeq, Aug 2010]

Expression

Ubiquitous expression in testis (RPKM 3.5), skin (RPKM 2.8) and 24 other tissues See more

Orthologs mouse all

Preferred Names

kelch-like protein 17

Names

actinfilin

kelch-like 17

Related articles in PubMed

1. Actinfilin, a brain-specific actin-binding protein in postsynaptic density. Chen Y, et al. J Biol Chem, 2002 Aug 23. PMID 12063253. The dynamic assembly and disassembly of actin-based cytoskeleton is closely linked to the changes in the postsynaptic density in both number and shape, which is thought to be important in forming long-term memory. Thus, regulation of actin filaments may play a critical role in contributing to the formation of long-term memory. Here, we report the cloning of actinfilin, a brain-specific Kelch protein, which interacts with F-actin. Actinfilin contains an amino-terminal POZ/BTB domain and carboxyl positioned six tandem Kelch repeats that presumably form six blades of beta-propeller structure of the Kelch domain. Co-immunoprecipitation analyses showed that the amino-terminal POZ domain mediated actinfilin-actinfilin interaction. The recombinant Kelch domain alone was sufficient to mediate binding to F-actin. Immunohistochemistry studies of rat brain sections suggested that actinfilin is broadly expressed in neurons of most regions of the brain. The subcellular localization of actinfilin was studied by biochemical fractionation and immunogold labeling. The results showed the postsynaptic density distribution of actinfilin. Together, these results indicate that actinfilin may be a key player in the actin-based neuronal function
2. Update on the Kelch-like (KLHL) gene family. Dhanoa BS, et al. Hum Genomics, 2013 May 15. PMID 23676014, Free PMC Article
3. Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Böhm D, et al. Oncol Rep, 2012 Aug. PMID 22664934, Free PMC Article
4. The DNA sequence and biological annotation of human chromosome 1. Gregory SG, et al. Nature, 2006 May 18. PMID 16710414
5. Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Bennett EJ, et al. Cell, 2010 Dec 10. PMID 21145461, Free PMC Article

See all (9) citations in PubMed

https://www.ncbi.nlm.nih.gov/pubmed/28912426
 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5599639/bin/41598_2017_10199_Fig1_HTML.jpg
Breast cancer is a complex disease consisting of four distinct molecular subtypes. DNA methylation-based (DNAm) studies in tumors are complicated further by disease heterogeneity. In the present study, we compared DNAm in breast tumors with normal-adjacent breast samples from The Cancer Genome Atlas (TCGA). We constructed models stratified by tumor stage and PAM50 molecular subtype and performed cell-type reference-free deconvolution to control for cellular heterogeneity. We identified nineteen differentially methylated gene regions (DMGRs) in early stage tumors across eleven genes (AGRN, C1orf170, FAM41C, FLJ39609, HES4, ISG15, KLHL17, NOC2L, PLEKHN1, SAMD11, WASH5P). These regions were consistently differentially methylated in every subtype and all implicated genes are localized to the chromosomal cytoband 1p36.3. Seventeen of these DMGRs were independently validated in a similar analysis of an external data set. The identification and validation of shared DNAm alterations across tumor subtypes in early stage tumors advances our understanding of common biology underlying breast carcinogenesis and may contribute to biomarker development. We also discuss evidence of the specific importance and potential function of 1p36 in cancer.