LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome.
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.
Mesh Terms:
1-Alkyl-2-acetylglycerophosphocholine Esterase, Animals, COS Cells, Central Nervous System, Centrosome, Embryo, Nonmammalian, Fungal Proteins, Gene Expression Regulation, Developmental, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Structure, Tertiary, RNA, Messenger, Sequence Homology, Amino Acid, Substrate Specificity, Tubulin, Two-Hybrid System Techniques, Xenopus
1-Alkyl-2-acetylglycerophosphocholine Esterase, Animals, COS Cells, Central Nervous System, Centrosome, Embryo, Nonmammalian, Fungal Proteins, Gene Expression Regulation, Developmental, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Structure, Tertiary, RNA, Messenger, Sequence Homology, Amino Acid, Substrate Specificity, Tubulin, Two-Hybrid System Techniques, Xenopus
Neuron
Date: Dec. 01, 2000
PubMed ID: 11163258
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