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Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein

PDZ motifs are modular protein–protein interaction domains, consisting of 80–120 amino acid residues, whose function appears to be the direction of intracellular proteins to multiprotein complexes. In skeletal muscle, there are a few known PDZ-domain proteins, which include neuronal nitric oxide syn...

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Autores principales: Faulkner, Georgine, Pallavicini, Alberto, Formentin, Elide, Comelli, Anna, Ievolella, Chiara, Trevisan, Silvia, Bortoletto, Gladis, Scannapieco, Paolo, Salamon, Michela, Mouly, Vincent, Valle, Giorgio, Lanfranchi, Gerolamo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1999
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3206570/
https://www.ncbi.nlm.nih.gov/pubmed/10427098
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author Faulkner, Georgine
Pallavicini, Alberto
Formentin, Elide
Comelli, Anna
Ievolella, Chiara
Trevisan, Silvia
Bortoletto, Gladis
Scannapieco, Paolo
Salamon, Michela
Mouly, Vincent
Valle, Giorgio
Lanfranchi, Gerolamo
author_facet Faulkner, Georgine
Pallavicini, Alberto
Formentin, Elide
Comelli, Anna
Ievolella, Chiara
Trevisan, Silvia
Bortoletto, Gladis
Scannapieco, Paolo
Salamon, Michela
Mouly, Vincent
Valle, Giorgio
Lanfranchi, Gerolamo
author_sort Faulkner, Georgine
collection PubMed
description PDZ motifs are modular protein–protein interaction domains, consisting of 80–120 amino acid residues, whose function appears to be the direction of intracellular proteins to multiprotein complexes. In skeletal muscle, there are a few known PDZ-domain proteins, which include neuronal nitric oxide synthase and syntrophin, both of which are components of the dystrophin complex, and actinin-associated LIM protein, which binds to the spectrin-like repeats of α-actinin-2. Here, we report the identification and characterization of a new skeletal muscle protein containing a PDZ domain that binds to the COOH-terminal region of α-actinin-2. This novel 31-kD protein is specifically expressed in heart and skeletal muscle. Using antibodies produced to a fragment of the protein, we can show its location in the sarcomere at the level of the Z-band by immunoelectron microscopy. At least two proteins, 32 kD and 78 kD, can be detected by Western blot analysis of both heart and skeletal muscle, suggesting the existence of alternative forms of the protein. In fact, several forms were found that appear to be the result of alternative splicing. The transcript coding for this Z-band alternatively spliced PDZ motif (ZASP) protein maps on chromosome 10q22.3-10q23.2, near the locus for infantile-onset spinocerebellar ataxia.
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spelling pubmed-32065702011-11-02 Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein Faulkner, Georgine Pallavicini, Alberto Formentin, Elide Comelli, Anna Ievolella, Chiara Trevisan, Silvia Bortoletto, Gladis Scannapieco, Paolo Salamon, Michela Mouly, Vincent Valle, Giorgio Lanfranchi, Gerolamo J Cell Biol Original Article PDZ motifs are modular protein–protein interaction domains, consisting of 80–120 amino acid residues, whose function appears to be the direction of intracellular proteins to multiprotein complexes. In skeletal muscle, there are a few known PDZ-domain proteins, which include neuronal nitric oxide synthase and syntrophin, both of which are components of the dystrophin complex, and actinin-associated LIM protein, which binds to the spectrin-like repeats of α-actinin-2. Here, we report the identification and characterization of a new skeletal muscle protein containing a PDZ domain that binds to the COOH-terminal region of α-actinin-2. This novel 31-kD protein is specifically expressed in heart and skeletal muscle. Using antibodies produced to a fragment of the protein, we can show its location in the sarcomere at the level of the Z-band by immunoelectron microscopy. At least two proteins, 32 kD and 78 kD, can be detected by Western blot analysis of both heart and skeletal muscle, suggesting the existence of alternative forms of the protein. In fact, several forms were found that appear to be the result of alternative splicing. The transcript coding for this Z-band alternatively spliced PDZ motif (ZASP) protein maps on chromosome 10q22.3-10q23.2, near the locus for infantile-onset spinocerebellar ataxia. The Rockefeller University Press 1999-07-26 /pmc/articles/PMC3206570/ /pubmed/10427098 Text en © 1999 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Faulkner, Georgine
Pallavicini, Alberto
Formentin, Elide
Comelli, Anna
Ievolella, Chiara
Trevisan, Silvia
Bortoletto, Gladis
Scannapieco, Paolo
Salamon, Michela
Mouly, Vincent
Valle, Giorgio
Lanfranchi, Gerolamo
Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein
title Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein
title_full Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein
title_fullStr Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein
title_full_unstemmed Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein
title_short Zasp: A New Z-Band Alternatively Spliced PDZ-Motif Protein
title_sort zasp: a new z-band alternatively spliced pdz-motif protein
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3206570/
https://www.ncbi.nlm.nih.gov/pubmed/10427098
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