CDKL5 belongs to the same molecular pathway of MeCP2 and it is responsible for the early-onset seizure variant of Rett syndrome

Francesca Mari(University of Siena), Sara Azimonti(University of Insubria), Ilaria Bertani(University of Insubria), Fabrizio Bolognese(University of Insubria), Elena Colombo(Vita-Salute San Raffaele University), Rossella Caselli(University of Siena), Elisa Scala(University of Siena), Ilaria Longo(University of Siena), Salvatore Grosso(University of Siena), Chiara Pescucci(University of Siena), Francesca Ariani(University of Siena), Giuseppe Hayek(Azienda Ospedaliera Universitaria Senese), Paolo Balestri(University of Siena), Anna Bergo(University of Insubria), Gianfranco Badaracco(University of Insubria), Michele Zappella(Azienda Ospedaliera Universitaria Senese), Vania Broccoli(IRCCS Ospedale San Raffaele), Alessandra Renieri(University of Siena), Charlotte Kilstrup‐Nielsen(University of Insubria), Nicoletta Landsberger(University of Insubria)
Human Molecular Genetics
May 25, 2005
Cited by 318Open Access
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Abstract

Rett syndrome (RTT) is a severe neurodevelopmental disorder almost exclusively affecting females and characterized by a wide spectrum of clinical manifestations. Most patients affected by classic RTT and a smaller percentage of patients with the milder form 'preserved speech variant' have either point mutations or deletions/duplications in the MECP2 gene. Recently, mutations in the CDKL5 gene, coding for a putative kinase, have been found in female patients with a phenotype overlapping with that of RTT. Here, we report two patients with the early seizure variant of RTT, bearing two novel CDKL5 truncating mutations, strengthening the correlation between CDKL5 and RTT. Considering the similar phenotypes caused by mutations in MECP2 and CDKL5, it has been suggested that the two genes play a role in common pathogenic processes. We show here that CDKL5 is a nuclear protein whose expression in the nervous system overlaps with that of MeCP2, during neural maturation and synaptogenesis. Importantly, we demonstrate that MeCP2 and CDKL5 interact both in vivo and in vitro and that CDKL5 is indeed a kinase, which is able to phosphorylate itself and to mediate MeCP2 phosphorylation, suggesting that they belong to the same molecular pathway. Furthermore, this paper contributes to the clarification of the phenotype associated with CDKL5 mutations and indicates that CDKL5 should be analyzed in each patient showing a clinical course similar to RTT but characterized by a lack of an early normal period due to the presence of seizures.


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