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The Journal of Neuroscience, June 11, 2008, 28(24):6111-6117; doi:10.1523/JNEUROSCI.1044-08.2008

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Brief Communications
Schwannomin-Interacting Protein-1 Isoform IQCJ-SCHIP-1 Is a Late Component of Nodes of Ranvier and Axon Initial Segments

Pierre-Marie Martin,^1,2,3 Michèle Carnaud,^1,2,3 Gontzal Garcia del Caño,^4,5,6 Marie Irondelle,^4,5 Theano Irinopoulou,^1,2,3 Jean-Antoine Girault,^1,2,3 Bénédicte Dargent,^4,5 and Laurence Goutebroze^1,2,3

¹Unité Mixte de Recherche-S 839, Inserm, ²Université Pierre et Marie Curie (UPMC), ³Institut du Fer à Moulin, Paris 75005, France, ⁴U641, Inserm, ⁵Université de la Méditerranée, Faculté de Médecine Secteur Nord, Institut Fédératif de Recherche 11, Marseille 13916, France, and ⁶Department of Neurosciences, Faculty of Pharmacy, University of the Basque Country, Vitoria-Gasteiz, 01006 Araba, Spain

Correspondence should be addressed to Laurence Goutebroze and Jean-Antoine Girault at the above address. Email: goutebro{at}fer-a-moulin.inserm.fr and Email: girault{at}fer-a-moulin.inserm.fr

Axon initial segments (AISs) and nodes of Ranvier (NRs) are essential regions for saltatory conduction of the action potential along the axon. These two domains are enriched in similar multimolecular complexes, which include voltage-gated sodium channels (Na_v), NF186 (neurofascin 186), NrCAM (neuron glia-related cell adhesion molecule), and cytoskeleton linkers ankyrin G (AnkG) and βIV-spectrin. Identification of novel members of these complexes is critical to better understand their formation, function, and maintenance. Here we report that IQCJ-SCHIP-1, a recently identified isoform of schwannomin-interacting protein-1 (SCHIP-1), is a novel component of both AISs and NRs in the central and peripheral nervous systems. We show that IQCJ-SCHIP-1 binds calmodulin in the absence of Ca²⁺ and is highly enriched at AISs and NRs. IQCJ-SCHIP-1 accumulation at AISs and NRs is a late event, suggesting that IQCJ-SCHIP-1 is likely to play a role in mature AISs and NRs rather than during their formation. IQCJ-SCHIP-1 was not detected at AISs in the absence of AnkG and interacted in vitro with this protein. IQCJ-SCHIP-1 was also absent from central NRs and AISs of quivering mice, which have a mutation of βIV-spectrin. We suggest that IQCJ-SCHIP-1 might participate, along with AnkG and βIV-spectrin, in the stabilization or function of the multimolecular complexes of AISs and NRs, possibly by participating in Ca²⁺-mediated responses.

Key words: myelinated fibers; schwannomin/merlin; calmodulin; ankyrin G; βIV-spectrin; voltage-gated sodium channels; language disorder

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Received Nov. 8, 2007; revised April 17, 2008; accepted April 22, 2008.

Correspondence should be addressed to Laurence Goutebroze and Jean-Antoine Girault at the above address. Email: goutebro{at}fer-a-moulin.inserm.fr and Email: girault{at}fer-a-moulin.inserm.fr

This article has been cited by other articles:

				A. Brechet, M.-P. Fache, A. Brachet, G. Ferracci, A. Baude, M. Irondelle, S. Pereira, C. Leterrier, and B. Dargent Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G J. Cell Biol., December 15, 2008; 183(6): 1101 - 1114. [Abstract] [Full Text] [PDF]

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