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XB-ART-55531
Science January 1, 2018; 362 (6411):

Dimerization quality control ensures neuronal development and survival.

Mena EL , Kjolby RAS , Saxton RA , Werner A , Lew BG , Boyle JM , Harland R , Rape M .


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 SCFFBXL17, which selectively binds and ubiquitylates BTB dimers of aberrant composition to trigger their clearance by proteasomal degradation. Underscoring the physiological importance of DQC, SCFFBXL17 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.

PubMed ID: 30190310
Article link: Science
Grant support: [+]
Genes referenced: bcl6 cul1 fbxl17 kbtbd8 keap1 klhl12 klhl13 klhl41 klhl9
Morpholinos: fbxl17 MO1 fbxl17 MO2 fbxl17 MO3 fbxl17 MO4 fbxl17 MO5

References :
Herhaus, Dimerization quality control via ubiquitylation. 2018, Pubmed


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