| Literature DB >> 29728705 |
Suzanna G M Frints1,2, Aysegul Ozanturk3, Germán Rodríguez Criado4, Ute Grasshoff5, Bas de Hoon6,7, Michael Field8, Sylvie Manouvrier-Hanu9,10, Scott E Hickey11,12, Molka Kammoun13, Karen W Gripp14, Claudia Bauer5, Christopher Schroeder5, Annick Toutain15,16, Theresa Mihalic Mosher11,12,17, Benjamin J Kelly17, Peter White12,17, Andreas Dufke5, Eveline Rentmeester6, Sungjin Moon3, Daniel C Koboldt12,17, Kees E P van Roozendaal18,19, Hao Hu20, Stefan A Haas21, Hans-Hilger Ropers20, Lucinda Murray8, Eric Haan22,23, Marie Shaw22, Renee Carroll22, Kathryn Friend24, Jan Liebelt23, Lynne Hobson24, Marjan De Rademaeker25, Joep Geraedts18,19, Jean-Pierre Fryns13, Joris Vermeesch13, Martine Raynaud15,16, Olaf Riess5, Joost Gribnau6, Nicholas Katsanis3, Koen Devriendt13, Peter Bauer5, Jozef Gecz22,26, Christelle Golzio3,27, Cristina Gontan6, Vera M Kalscheuer28.
Abstract
RLIM, also known as RNF12, is an X-linked E3 ubiquitin ligase acting as a negative regulator of LIM-domain containing transcription factors and participates in X-chromosome inactivation (XCI) in mice. We report the genetic and clinical findings of 84 individuals from nine unrelated families, eight of whom who have pathogenic variants in RLIM (RING finger LIM domain-interacting protein). A total of 40 affected males have X-linked intellectual disability (XLID) and variable behavioral anomalies with or without congenital malformations. In contrast, 44 heterozygous female carriers have normal cognition and behavior, but eight showed mild physical features. All RLIM variants identified are missense changes co-segregating with the phenotype and predicted to affect protein function. Eight of the nine altered amino acids are conserved and lie either within a domain essential for binding interacting proteins or in the C-terminal RING finger catalytic domain. In vitro experiments revealed that these amino acid changes in the RLIM RING finger impaired RLIM ubiquitin ligase activity. In vivo experiments in rlim mutant zebrafish showed that wild type RLIM rescued the zebrafish rlim phenotype, whereas the patient-specific missense RLIM variants failed to rescue the phenotype and thus represent likely severe loss-of-function mutations. In summary, we identified a spectrum of RLIM missense variants causing syndromic XLID and affecting the ubiquitin ligase activity of RLIM, suggesting that enzymatic activity of RLIM is required for normal development, cognition and behavior.Entities:
Mesh:
Substances:
Year: 2018 PMID: 29728705 DOI: 10.1038/s41380-018-0065-x
Source DB: PubMed Journal: Mol Psychiatry ISSN: 1359-4184 Impact factor: 15.992