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Merck
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  • Biallelic loss of human CTNNA2, encoding αN-catenin, leads to ARP2/3 complex overactivity and disordered cortical neuronal migration.

Biallelic loss of human CTNNA2, encoding αN-catenin, leads to ARP2/3 complex overactivity and disordered cortical neuronal migration.

Nature genetics (2018-07-18)
Ashleigh E Schaffer, Martin W Breuss, Ahmet Okay Caglayan, Nouriya Al-Sanaa, Hind Y Al-Abdulwahed, Hande Kaymakçalan, Cahide Yılmaz, Maha S Zaki, Rasim O Rosti, Brett Copeland, Seung Tae Baek, Damir Musaev, Eric C Scott, Tawfeg Ben-Omran, Ariana Kariminejad, Hulya Kayserili, Faezeh Mojahedi, Majdi Kara, Na Cai, Jennifer L Silhavy, Seham Elsharif, Elif Fenercioglu, Bruce A Barshop, Bulent Kara, Rengang Wang, Valentina Stanley, Kiely N James, Rahul Nachnani, Aneesha Kalur, Hisham Megahed, Faruk Incecik, Sumita Danda, Yasemin Alanay, Eissa Faqeih, Gia Melikishvili, Lobna Mansour, Ian Miller, Biayna Sukhudyan, Jamel Chelly, William B Dobyns, Kaya Bilguvar, Rami Abou Jamra, Murat Gunel, Joseph G Gleeson
摘要

Neuronal migration defects, including pachygyria, are among the most severe developmental brain defects in humans. Here, we identify biallelic truncating mutations in CTNNA2, encoding αN-catenin, in patients with a distinct recessive form of pachygyria. CTNNA2 was expressed in human cerebral cortex, and its loss in neurons led to defects in neurite stability and migration. The αN-catenin paralog, αE-catenin, acts as a switch regulating the balance between β-catenin and Arp2/3 actin filament activities1. Loss of αN-catenin did not affect β-catenin signaling, but recombinant αN-catenin interacted with purified actin and repressed ARP2/3 actin-branching activity. The actin-binding domain of αN-catenin or ARP2/3 inhibitors rescued the neuronal phenotype associated with CTNNA2 loss, suggesting ARP2/3 de-repression as a potential disease mechanism. Our findings identify CTNNA2 as the first catenin family member with biallelic mutations in humans, causing a new pachygyria syndrome linked to actin regulation, and uncover a key factor involved in ARP2/3 repression in neurons.