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Publication : LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome.

First Author  Feng Y Year  2000
Journal  Neuron Volume  28
Issue  3 Pages  665-79
PubMed ID  11163258 Mgi Jnum  J:66488
Mgi Id  MGI:1928549 Doi  10.1016/s0896-6273(00)00145-8
Citation  Feng Y, et al. (2000) LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron 28(3):665-79
abstractText  LIS1, a microtubule-associated protein, is required for neuronal migration, but the precise mechanism of LIS1 function is unknown. We identified a LIS1 interacting protein encoded by a mouse homolog of NUDE, a nuclear distribution gene in A. nidulans and a multicopy suppressor of the LIS1 homolog, NUDF. mNudE is located in the centrosome or microtubule organizing center (MTOC), and interacts with six different centrosomal proteins. Overexpression of mNudE dissociates gamma-tubulin from the centrosome and disrupts microtubule organization. Missense mutations that disrupt LIS1 function block LIS1-mNudE binding. Moreover, misexpression of the LIS1 binding domain of mNudE in Xenopus embryos disrupts the architecture and lamination of the CNS. Thus, LIS1-mNudE interactions may regulate neuronal migration through dynamic reorganization of the MTOC.
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