Fbxo45 Forms a Novel Ubiquitin Ligase Complex and Is Required for Neuronal Development-Reference-Cited by-同舟云学术

Fbxo45 Forms a Novel Ubiquitin Ligase Complex and Is Required for Neuronal Development

Published:2009-07 Issue:13 Volume:29 Page:3529-3543
ISSN:0270-7306
Container-title:Molecular and Cellular Biology
language:en
Short-container-title:Mol Cell Biol

Author:

Saiga Toru¹²,Fukuda Takaichi³,Matsumoto Masaki¹²,Tada Hirobumi⁴⁵,Okano Hirotaka James⁵,Okano Hideyuki⁵,Nakayama Keiichi I.¹²

Affiliation:

1. Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan

2. CREST, Japan Science and Technology Agency, Kawaguchi, Saitama 332-0012, Japan

3. Department of Anatomy and Neurobiology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan

4. Physiology and Neuroendocrinology, Yokohama City University Graduate School of Medicine, Yokohama 236-0004, Japan

5. Department of Physiology, Keio University School of Medicine, Shinjuku, Tokyo 160-8582, Japan

Abstract

ABSTRACT Fbxo45 is an F-box protein that is restricted to the nervous system. Unlike other F-box proteins, Fbxo45 was found not to form an SCF complex as a result of an amino acid substitution in the consensus sequence for Cul1 binding. Proteomics analysis revealed that Fbxo45 specifically associates with PAM (protein associated with Myc), a RING finger-type ubiquitin ligase. Mice deficient in Fbxo45 were generated and found to die soon after birth as a result of respiratory distress. Fbxo45 − / − embryos show abnormal innervation of the diaphragm, impaired synapse formation at neuromuscular junctions, and aberrant development of axon fiber tracts in the brain. Similar defects are also observed in mice lacking Phr1 (mouse ortholog of PAM), suggesting that Fbxo45 and Phr1 function in the same pathway. In addition, neuronal migration was impaired in Fbxo45 − / − mice. These results suggest that Fbxo45 forms a novel Fbxo45-PAM ubiquitin ligase complex that plays an important role in neural development.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

Link

https://journals.asm.org/doi/pdf/10.1128/MCB.00364-09

Reference49 articles.

1. Bloom, A. J., B. R. Miller, J. R. Sanes, and A. DiAntonio. 2007. The requirement for Phr1 in CNS axon tract formation reveals the corticostriatal boundary as a choice point for cortical axons. Genes Dev.21:2593-2606.

2. Evidence for a Conserved Function in Synapse Formation Reveals Phr1 as a Candidate Gene for Respiratory Failure in Newborn Mice

3. Cardozo, T., and M. Pagano. 2004. The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell Biol.5:739-751.

4. Cenciarelli, C., D. S. Chiaur, D. Guardavaccaro, W. Parks, M. Vidal, and M. Pagano. 1999. Identification of a family of human F-box proteins. Curr. Biol.9:1177-1179.

5. Collins, C. A., Y. P. Wairkar, S. L. Johnson, and A. DiAntonio. 2006. Highwire restrains synaptic growth by attenuating a MAP kinase signal. Neuron51:57-69.

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