The muscle Z band: lessons in stress management

Vigoreaux, Jim O.

doi:10.1007/bf00123477

Cited by 105 publications

(64 citation statements)

References 103 publications

(161 reference statements)

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“…Z discs vary in structure and width in different tissues and fibre types, and during development. 24 The alternative use of Figure 5 20 different nebulin transcripts from adult human tibialis anterior muscle.…”

Section: Discussionmentioning

confidence: 99%

Complete genomic structure of the human nebulin gene and identification of alternatively spliced transcripts

et al. 2004

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The giant nebulin protein is a fundamental structural component of the thin filaments of the striated muscle sarcomere. Nebulin binds to actin and the size of nebulin correlates with actin filament length, suggesting that nebulin may determine the length of the thin filaments during myofibrillogenesis. We have previously described the genomic organization of the 3 0 end of the nebulin gene (NEB), and identified 18 different NEB mutations in patients with autosomal recessive nemaline myopathy. Here we present the genomic organization of the entire nebulin gene, and the identification of numerous alternatively spliced mRNAs. The gene comprises 183 exons spanning 249 kb of the genomic sequence. The translation initiation codon is in exon 3, and the stop codon and the 3 0 UTR are in exon 183. There are four regions with alternatively spliced exons, that is, exons 63 -66, 82-105, 143 -144 and 166 -177, giving rise to a number of different transcripts. The alternatively spliced exons 143 -144 give rise to two different transcripts varying between muscle types and between muscles of different developmental stages. The alternatively spliced exons 166 -177 express at least 20 different transcripts in adult human tibialis anterior muscle alone. Preliminary results show several transcripts in both of the two remaining alternatively spliced regions. Extensive alternative splicing of NEB may explain why nemaline myopathy patients with homozygous truncating mutations show expression of the carboxy-terminus of the nebulin protein contrary to expectations . The use of alternative transcripts might also explain why severe phenotypes are rare among patients with two truncating mutations.

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Section: Discussionmentioning

confidence: 99%

Complete genomic structure of the human nebulin gene and identification of alternatively spliced transcripts

et al. 2004

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“…In skeletal muscle fibers, desmin intermediate filaments are distributed at the level of the Z-disc, thus suggesting that they may play a role in structural integrity, especially in alignment of adjacent myofibrils in lateral register (Lazarides, 1980;Ishikawa, 1983;Vigoreaux, 1994). More recently, the role of plectin molecules in mechanical linkage between desmin intermediate filaments and the Z-discs has been unequivocally proved (Hijikata et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Localization of Plectin and Other Related Proteins along the Sarcolemma in Smooth Muscle Cells of Rat Colon.

Tanaka

Hijikata

Murakami

et al. 2001

Cell Struct. Funct.

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ABSTRACT. Plectin is a versatile linker protein which is associated with various types of cytoskeletal components and/or filaments including intermediate filaments. To better understand the functional roles of plectin in smooth muscle cells, we examined the distribution of plectin and other related proteins in rat colon smooth muscles by confocal laser and electron microscopy. The sarcolemma of smooth muscle cells exhibits two ultrastructurally distinct domains, domains associated with dense plaques and caveola-rich domains. Staining with anti-plectin and anti-desmin antibodies showed that plectin was localized along the sarcolemma in an intermittent manner and desmin was distributed in the sarcoplasm and intermittently at the cell periphery where it was codistributed with desmin. Plectin exhibited complementary and non-overlapping distribution to caveolin-1 and dystrophin, components of caveola domains, whereas plectin was codistributed with vinculin, talin and integrin > > > >1, components of dense plaques. Plectin was also codistributed with > > > >2-chain laminin but not with > > > >1-chain laminin. Electron microscopic observations on the sarcolemma revealed close association of intermediate filaments with dense plaques. Correlated confocal and electron microscopy clearly demonstrated that anti-plectin fluorescence corresponded to dense plaques but not to caveola domains in electron microscopic images. These findings indicate that plectin is confined to dense plaques to which desmin intermediate filaments may be anchored in rat colon smooth muscle cells.Key words: smooth muscle/plectin/dense plaques/confocal laser microscopy/electron microscopy/caveolin-1 Plectin, a member of the plakin family, is a versatile cytoskeletal linker protein and occurs in a wide variety of tissues and cell types, in which plectin codistributes with various types of intermediate filament proteins, such as vimentin, cytokeratins, desmin and glial fibrillary acidic (GFA) protein (Wiche et al., 1983Hieda et al., 1992;Errante et al., 1994;Yaoita et al., 1996;Svitkina et al., 1996;Eger et al., 1997;Foisner et al., 1988Foisner et al., , 1991. Plectin is located at the intermediate filament-plasma membrane interface, such as hemidesmosomes, desmosomes, and cardiac muscle intercalated discs. Plectin appears to act as molecular bridges between intermediate filaments and actin filaments or microtubules, as shown by whole-mount electron microscopy (Wiche et al., 1982(Wiche et al., , 1983. More recently, plectin has been shown to link intermediate filaments to the Z-discs in skeletal muscle fibers (Hijikata et al., 1999). Consistent with these variable locations, plectin possesses the binding capacity to multiple cytoskeletal proteins, such as =-spectrin (fodrin), high molecular mass microtubule-associated proteins and integrin >4 (Hermann and Wiche, 1987;Svitkina et al., 1996;Rezniczek et al., 1998). The strategic localization and versatile binding property of plectin suggest that it plays significant functional roles in the structural inte...

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“…Actin anchorage sites in muscle act as docking sites for multiple protein complexes involved in both tethering the contractile machinery and coupling it to the muscle cell membrane (for review, see Vigoreaux, 1994).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of the Caenorhabditis elegans ALP/Enigma gene alp‐1

McKeown

Han

Beckerle

2005

Developmental Dynamics

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Members of the ALP/Enigma family of PDZ-LIM proteins play a role in cytoskeletal anchorage and mutations in at least one member of this family are associated with human cardiomyopathy. Here, we describe the analysis of the Caenorhabditis elegans alp-1 gene. alp-1 is predicted to encode the entire nematode ALP/Enigma protein family, consisting of one ALP-related protein with a single LIM domain and three Enigma-like proteins containing four LIM domains. We demonstrate that the ALP-1 proteins are expressed in muscle cells, where they localize to actin anchorage and muscle attachment sites. We show that the PDZ domain of the ALP-1 proteins is sufficient to target the protein to the dense bodies, which are important actin anchorage sites in C. elegans body wall muscle. We demonstrate that the C. elegans ALP/Enigma proteins are also localized to cell-cell junctions and to both epithelial and muscle cell nuclei. These findings suggest new roles for the ALP/Enigma protein family that may lead to the understanding of their involvement in cardiomyopathy. Developmental Dynamics 235:530 -538, 2006.

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The muscle Z band: lessons in stress management

Cited by 105 publications

References 103 publications

Complete genomic structure of the human nebulin gene and identification of alternatively spliced transcripts

Complete genomic structure of the human nebulin gene and identification of alternatively spliced transcripts

Localization of Plectin and Other Related Proteins along the Sarcolemma in Smooth Muscle Cells of Rat Colon.

Molecular characterization of the Caenorhabditis elegans ALP/Enigma gene alp‐1

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