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

Yuanyi Feng, Eric C. Olson, P. Todd Stukenberg, Lisa A. Flanagan, Marc W. Kirschner, Christopher A. Walsh*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

239 Scopus citations

Abstract

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 γ-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.

Original languageEnglish (US)
Pages (from-to)665-679
Number of pages15
JournalNeuron
Volume28
Issue number3
DOIs
StatePublished - 2000

ASJC Scopus subject areas

  • Neuroscience(all)

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