2.50
Hdl Handle:
http://hdl.handle.net/10033/18825
Title:
Raver1 is an integral component of muscle contractile elements.
Authors:
Zieseniss, Anke; Schroeder, Ulrich; Buchmeier, Sabine; Schoenenberger, Cora-Ann; van den Heuvel, Joop; Jockusch, Brigitte M; Illenberger, Susanne
Abstract:
Raver1, a ubiquitously expressed protein, was originally identified as a ligand for metavinculin, the muscle-specific isoform of the microfilament-associated protein vinculin. The protein resides primarily in the nucleus, where it colocalises and may interact with polypyrimidine-tract-binding protein, which is involved in alternative splicing processes. During skeletal muscle differentiation, raver1 translocates to the cytoplasm and eventually targets the Z-line of sarcomeres. Here, it colocalises with metavinculin, vinculin and alpha-actinin, all of which have biochemically been identified as raver1 ligands. To obtain more information about the potential role of raver1 in muscle structure and function, we have investigated its distribution and fine localisation in mouse striated and smooth muscle, by using three monoclonal antibodies that recognise epitopes in different regions of the raver1 protein. Our immunofluorescence and immunoelectron-microscopic results indicate that the cytoplasmic accumulation of raver1 is not confined to skeletal muscle but also occurs in heart and smooth muscle. Unlike vinculin and metavinculin, cytoplasmic raver1 is not restricted to costameres but additionally represents an integral part of the sarcomere. In isolated myofibrils and in ultrathin sections of skeletal muscle, raver1 has been found concentrated at the I-Z-I band. A minor fraction of raver1 is present in the nuclei of all three types of muscle. These data indicate that, during muscle differentiation, raver1 might link gene expression with structural functions of the contractile machinery of muscle.
Affiliation:
Cell Biology, Zoological Institute, Technical University of Braunschweig, Biocentre, Spielmannstrasse 7, 38092 Braunschweig, Germany.
Citation:
Raver1 is an integral component of muscle contractile elements. 2007, 327 (3):583-94 Cell Tissue Res.
Journal:
Cell and tissue research
Issue Date:
Mar-2007
URI:
http://hdl.handle.net/10033/18825
DOI:
10.1007/s00441-006-0322-1
PubMed ID:
17096167
Type:
Article
Language:
en
ISSN:
0302-766X
Appears in Collections:
Publications from Division of Molekulare Struktur Biologie (MOSB)

Full metadata record

DC FieldValue Language
dc.contributor.authorZieseniss, Anke-
dc.contributor.authorSchroeder, Ulrich-
dc.contributor.authorBuchmeier, Sabine-
dc.contributor.authorSchoenenberger, Cora-Ann-
dc.contributor.authorvan den Heuvel, Joop-
dc.contributor.authorJockusch, Brigitte M-
dc.contributor.authorIllenberger, Susanne-
dc.date.accessioned2008-02-21T13:41:29Z-
dc.date.available2008-02-21T13:41:29Z-
dc.date.issued2007-03-
dc.identifier.citationRaver1 is an integral component of muscle contractile elements. 2007, 327 (3):583-94 Cell Tissue Res.en
dc.identifier.issn0302-766X-
dc.identifier.pmid17096167-
dc.identifier.doi10.1007/s00441-006-0322-1-
dc.identifier.urihttp://hdl.handle.net/10033/18825-
dc.description.abstractRaver1, a ubiquitously expressed protein, was originally identified as a ligand for metavinculin, the muscle-specific isoform of the microfilament-associated protein vinculin. The protein resides primarily in the nucleus, where it colocalises and may interact with polypyrimidine-tract-binding protein, which is involved in alternative splicing processes. During skeletal muscle differentiation, raver1 translocates to the cytoplasm and eventually targets the Z-line of sarcomeres. Here, it colocalises with metavinculin, vinculin and alpha-actinin, all of which have biochemically been identified as raver1 ligands. To obtain more information about the potential role of raver1 in muscle structure and function, we have investigated its distribution and fine localisation in mouse striated and smooth muscle, by using three monoclonal antibodies that recognise epitopes in different regions of the raver1 protein. Our immunofluorescence and immunoelectron-microscopic results indicate that the cytoplasmic accumulation of raver1 is not confined to skeletal muscle but also occurs in heart and smooth muscle. Unlike vinculin and metavinculin, cytoplasmic raver1 is not restricted to costameres but additionally represents an integral part of the sarcomere. In isolated myofibrils and in ultrathin sections of skeletal muscle, raver1 has been found concentrated at the I-Z-I band. A minor fraction of raver1 is present in the nuclei of all three types of muscle. These data indicate that, during muscle differentiation, raver1 might link gene expression with structural functions of the contractile machinery of muscle.en
dc.language.isoenen
dc.subject.meshActinsen
dc.subject.meshAnimalsen
dc.subject.meshCarrier Proteinsen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshMiceen
dc.subject.meshMicroscopy, Immunoelectronen
dc.subject.meshMuscle Contractionen
dc.subject.meshMuscle, Skeletalen
dc.subject.meshMuscle, Smoothen
dc.subject.meshNuclear Proteinsen
dc.subject.meshSarcomeresen
dc.subject.meshVinculinen
dc.titleRaver1 is an integral component of muscle contractile elements.en
dc.typeArticleen
dc.contributor.departmentCell Biology, Zoological Institute, Technical University of Braunschweig, Biocentre, Spielmannstrasse 7, 38092 Braunschweig, Germany.en
dc.identifier.journalCell and tissue researchen

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