BTB domain mutations perturbing KCTD15 oligomerisation cause a distinctive frontonasal dysplasia syndrome

Conclusion
BTB domain substitutions in KCTD1 and KCTD15 cause clinically overlapping phenotypes involving craniofacial abnormalities and cutis aplasia. The structural analyses demonstrate that missense substitutions act through a dominant negative mechanism by disrupting the higher order structure of the KCTD15 protein complex.

Source: Journal of Medical Genetics - April 19, 2024 Category: Genetics & Stem Cells Authors: Miller, K. A., Cruz Walma, D. A., Pinkas, D. M., Tooze, R. S., Bufton, J. C., Richardson, W., Manning, C. E., Hunt, A. E., Cros, J., Hartill, V., Parker, M. J., McGowan, S. J., Twigg, S. R. F., Chalk, R., Staunton, D., Johnson, D., Wilkie, A. O. M., Bullo Tags: Open access Novel disease loci Source Type: research