FBXL17, (5q21.3), BTB-dimerisaatioitten kontrollantti, CLR1 adaptori, F-box motiivi, SCF- kompleksi (SKP1, CUL1, F-boxproteiinit)

https://www.ncbi.nlm.nih.gov/pubmed/30190310/

Official Symbol

FBXL17

Official Full Name

F-box and leucine rich repeat protein 17 p

Also known as

Fbl17; Fbx13; FBXO13

Summary

Members of the F-box protein family, such as FBXL17, are characterized by an approximately 40-amino acid F-box motif. SCF complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM 603134), and F-box proteins, act as protein-ubiquitin ligases. F-box proteins interact with SKP1 through the F box, and they interact with ubiquitination targets through other protein interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied by OMIM, Mar 2008]

Expression

Ubiquitous expression in thyroid (RPKM 4.5), brain (RPKM 4.2) and 25 other tissues See more

Ref.

'Science. 2018 Oct 12;362(6411). pii: eaap8236. doi: 10.1126/science.aap8236. Epub 2018 Sep 6.

Dimerization quality control ensures neuronal development and survival.

. Abstract

Aberrant complex formation by recurrent interaction modules, such as BTB domains, leucine zippers, or coiled coils, can disrupt signal transduction, yet whether cells detect and eliminate complexes of irregular composition is unknown. By searching for regulators of the BTB family, we discovered a quality control pathway that ensures functional dimerization [dimerization quality control (DQC)]. Key to this network is the E3 ligase SCF^FBXL17, which selectively binds and ubiquitylates BTB dimers of aberrant composition to trigger their clearance by proteasomal degradation. Underscoring the physiological importance of DQC, SCF^FBXL17 is required for the differentiation, function, and survival of neural crest and neuronal cells. We conclude that metazoan organisms actively monitor BTB dimerization, and we predict that distinct E3 ligases similarly control complex formation by other recurrent domains.

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