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Originally published In Press as doi:10.1074/jbc.M000439200 on March 16, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15851-15860, May 26, 2000
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gamma 1- and gamma 2-Syntrophins, Two Novel Dystrophin-binding Proteins Localized in Neuronal Cells*

Giulio PilusoDagger , Massimiliano Mirabella§, Enzo Ricci§||, Angela BelsitoDagger , Ciro AbbondanzaDagger , Serenella Servidei§, Annibale Alessandro PucaDagger **, Pietro Tonali§, Giovanni Alfredo PucaDagger , and Vincenzo NigroDagger Dagger Dagger

From the Dagger  Istituto di Patologia Generale ed Oncologia, Facoltà di Medicina, Seconda Università degli Studi di Napoli, 80138 Napoli, Italy, the § Istituto di Neurologia, Università Cattolica "A. Gemelli," Roma 00168, Italy, the  Center for Neuromuscular Diseases, Unione Italiana Lotta alla Distrofia Muscolare-Rome Section, Roma 00167, Italy, and the ** Division of Genetics, Children's Hospital, Boston, Massachusetts 02115

Dystrophin is the scaffold of a protein complex, disrupted in inherited muscular dystrophies. At the last 3' terminus of the gene, a protein domain is encoded, where syntrophins are tightly bound. These are a family of cytoplasmic peripheral membrane proteins. Three genes have been described encoding one acidic (alpha 1) and two basic (beta 1 and beta 2) proteins of ~57-60 kDa. Here, we describe the characterization of two novel putative members of the syntrophin family, named gamma 1- and gamma 2-syntrophins. The human gamma 1-syntrophin gene is composed of 19 exons and encodes a brain-specific protein of 517 amino acids. The human gamma 2-syntrophin gene is composed of at least 17 exons, and its transcript is expressed in brain and, to a lesser degree, in other tissues. We mapped the gamma 1-syntrophin gene to human chromosome 8q11 and the gamma 2-syntrophin gene to chromosome 2p25. Yeast two-hybrid experiments and pull-down studies showed that both proteins can bind the C-terminal region of dystrophin and related proteins. We raised antibodies against these proteins and recognized expression in both rat and human central neurons, coincident with RNA in situ hybridization of adjacent sections. Our present findings suggest a differentiated role of a modified dystrophin-associated complex in the central nervous system.

* This work was supported in part by Telethon-Italy and Ministero delle'Università e della Ricerca Scientifica e Tecnologica.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ003030 and AJ003029.

|| Supported in part by a grant from the Ministero Università e Ricerca Scientifica.

Dagger Dagger To whom correspondence should be addressed: Ist. di Patologia Generale e Oncologia, Facoltà di Medicina, Seconda Università degli Studi di Napoli, Larghetto S. Aniello a Caponapoli 2, 80138 Napoli, Italy. Tel.: 39081-5665675; Fax: 39081-5665695; E-mail: vincenzo.nigro@unina2.it.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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