Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24.

Ahn, Andrew H.; Yoshida, Motoaki; Anderson, Marydilys S.; Feener, Chris A.; Selig, Sara; Hagiwara, Yasuko; Ozawa, Eijiro; Kunkel, Louis M.

doi:10.1073/pnas.91.10.4446

Cited by 128 publications

(99 citation statements)

References 26 publications

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“…The sequences of these clones showed that they code for truncated forms of already known proteins. The product of clone 15 is highly homologous to the PSD-95 protein (Brenman et al, 1996) and that of clone 43 to the b1-syntrophin (Ahn et al, 1994). Clone 15 encodes a protein including only the PDZ1 and PDZ2 domains, but lacking the PDZ3, SH3 and guanylate kinase domains present in the carboxy-terminal part of PSD-95.…”

Section: Binding Of Tax To Pdz Proteinsmentioning

confidence: 99%

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

et al. 1998

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Infection by HTLV-1 has been correlated with the appearance of various proliferative or degenerative diseases. Some of these disorders have been observed in transgenic mice expressing the Tax protein, which is known to transactivate various viral and cellular promoters through interactions with several transcription factors. In this study we show that the C-terminus of this viral oncoprotein represents a motif permitting binding of Tax to the PDZ domains of several cellular proteins. A two-hybrid screen with Tax as bait indeed yielded complementary DNAs coding for six proteins including PDZ domains. Two of them correspond to truncated forms of the PSD-95 and b1-syntrophin proteins, another clone codes for a protein homologous to the product of the C. elegans gene lin-7. The other three clones code for new human members of the PDZ family of cellular proteins. The interaction of Tax with the products of these clones was con®rmed by immunoprecipitation assays in mammalian cells, and analysis of various mutants of Tax established the importance of the Cterminal amino acids for several of these interactions. These data suggest that Tax could perturb the normal function of targeted cellular proteins by strongly interacting with their PDZ domains.

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Section: Binding Of Tax To Pdz Proteinsmentioning

confidence: 99%

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

et al. 1998

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“…A third subcomplex of the dystrophin-associated protein complex involves ␣-dystrobrevin (10)(11)(12) and the syntrophins (␣1, ␤1, and ␤2) (13)(14)(15). These intracellular proteins directly bind to dystrophin (16,17).…”

mentioning

confidence: 99%

Desmuslin, an intermediate filament protein that interacts with α-dystrobrevin and desmin

Mizuno

Thompson

Guyon

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

147

166

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Dystrobrevin is a component of the dystrophin-associated protein complex and has been shown to interact directly with dystrophin, ␣1-syntrophin, and the sarcoglycan complex. The precise role of ␣-dystrobrevin in skeletal muscle has not yet been determined. To study ␣-dystrobrevin's function in skeletal muscle, we used the yeast two-hybrid approach to look for interacting proteins. Three overlapping clones were identified that encoded an intermediate filament protein we subsequently named desmuslin (DMN). Sequence analysis revealed that DMN has a short N-terminal domain, a conserved rod domain, and a long C-terminal domain, all common features of type 6 intermediate filament proteins. A positive interaction between DMN and ␣-dystrobrevin was confirmed with an in vitro coimmunoprecipitation assay. By Northern blot analysis, we find that DMN is expressed mainly in heart and skeletal muscle, although there is some expression in brain. Western blotting detected a 160-kDa protein in heart and skeletal muscle. Immunofluorescent microscopy localizes DMN in a stripe-like pattern in longitudinal sections and in a mosaic pattern in cross sections of skeletal muscle. Electron microscopic analysis shows DMN colocalized with desmin at the Z-lines. Subsequent coimmunoprecipitation experiments confirmed an interaction with desmin. Our findings suggest that DMN may serve as a direct linkage between the extracellular matrix and the Z-discs (through plectin) and may play an important role in maintaining muscle cell integrity.T he severe muscle wasting disorder, Duchenne muscular dystrophy, is caused by abnormalities in the dystrophin gene (1). The dystrophin protein is expressed in heart and skeletal muscle, where it is part of the dystrophin-associated protein complex. Dystrophin's N-terminal domain binds to actin, whereas the WW domain and the total cysteine-rich domain bind to ␤-dystroglycan (2), a component of the dystroglycan subcomplex. This subcomplex links to laminin, a major component of the basal membrane, thereby forming the linkage between an intracellular protein, actin, and the extracellular matrix.A second subcomplex of the dystrophin-associated protein complex includes four transmembrane proteins (␣-, ␤-, ␥-, and ␦-sarcoglycan) (3). Each has been shown to be involved in different forms of limb-girdle muscular dystrophy (LGMD 2D, 2E, 2C, and 2F) (4-8). ␣-Sarcoglycan is a type 1 transmembrane protein and is expressed in heart and skeletal muscle. ␤-, ␥-, and ␦-sarcoglycans are type 2 transmembrane proteins containing a cluster of cysteine residues in their extracellular domains. These four proteins form the sarcoglycan complex, which is thought to be involved in some type of signaling pathway (9).A third subcomplex of the dystrophin-associated protein complex involves ␣-dystrobrevin (10-12) and the syntrophins (␣1, ␤1, and ␤2) (13-15). These intracellular proteins directly bind to dystrophin (16,17). In addition, the N-terminal region of ␣-dystrobrevin associates with the sarcoglycan complex (18). There are at least ...

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“…Using partial peptide sequences generated from proteolytic digestion of the rabbit 50-kDa DAP, Roberds et al (13) identified a cDNA encoding the rabbit 50-kDa DAP and termed it adhalin. Isoelectric focusing analysis of the smaller components of the glycoprotein complex has suggested that the 35-kDa DAP may be heterogeneous (8).Dystroglycan and the syntrophins are expressed in tissues that lack the full-length dystrophin (10)(11)(12). This has raised speculation that in vivo, dystroglycan and the syntrophins may interact with proteins other than dystrophin.…”

mentioning

confidence: 99%

“…Dystroglycan and the syntrophins are expressed in tissues that lack the full-length dystrophin (10)(11)(12). This has raised speculation that in vivo, dystroglycan and the syntrophins may interact with proteins other than dystrophin.…”

mentioning

confidence: 99%

“…These include the 156-and 43-kDa glycoproteins, together named dystroglycan, that are produced from one transcript encoded by a single gene on chromosome 3p21 (9,10). Three separate genes encode the 59-kDa nonglycosylated members of the complex, called syntrophins (11,12). Three additional proteins (50, 35, and 25 kDa) also participate in dystrophin's membrane interaction (6)(7)(8)13).…”

mentioning

confidence: 99%

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Human adhalin is alternatively spliced and the gene is located on chromosome 17q21.

McNally

Yoshida

Mizuno

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Mutations in the dystrophin gene cause the X chromosome-linked, recessive Duchenne and Becker muscular dystrophies. Dystrophin, a large cytoskeletal protein, copurifles with a complex of dystrophin-aclated proteins which serve to anchor dystrophin to the sarcolemma. One of these associated proteins, adhalin, has been implicated as a candidate for severe childhood autosomal recessive muscular dystrophy (SCARMD) due to absence of anti-adhalin sning in muscle biopsy samples taken from SCARMD patients. Furthermore, the Duchenne-like dystrophic phenotype seen in the SCARMD families was shown to be tightly linked to chromosome 13 markers. To determine the genetic mutation responsible for autosomal dystrophy, we characterized the human adhalin gene. Contrary to our expectation, human adhalin was mapped to chromosome 17q21, excluding adhalin as the gene causing chromosome 13-associated SCARMD. Additionaily, a splice form of adhalin message was found that predicts a 35-kDa nontransmembrane adhalin. The expression of both adhalin splice forms is exclusively restricted to striated muscle, unlike other components of the dystrophin-glycoprotein complex.Genetic analyses of patients with Duchenne and Becker muscular dystrophy (DMD/BMD) have demonstrated a correlation between mutations in dystrophin's carboxyl terminus and a more severe clinical course (1). The carboxyl terminus of dystrophin binds a complex of dystrophinassociated proteins (DAPs), and components of this glycoprotein complex are decreased in DMD (2-5). Several DAPs have been identified by virtue of their copurification with dystrophin (6-8). These include the 156-and 43-kDa glycoproteins, together named dystroglycan, that are produced from one transcript encoded by a single gene on chromosome 3p21 (9,10). Three separate genes encode the 59-kDa nonglycosylated members of the complex, called syntrophins (11,12). Three additional proteins (50, 35, and 25 kDa) also participate in dystrophin's membrane interaction (6-8, 13). Using partial peptide sequences generated from proteolytic digestion of the rabbit 50-kDa DAP, Roberds et al. (13) identified a cDNA encoding the rabbit 50-kDa DAP and termed it adhalin. Isoelectric focusing analysis of the smaller components of the glycoprotein complex has suggested that the 35-kDa DAP may be heterogeneous (8).Dystroglycan and the syntrophins are expressed in tissues that lack the full-length dystrophin (10)(11)(12). This has raised speculation that in vivo, dystroglycan and the syntrophins may interact with proteins other than dystrophin. In vitro, syntrophin binds the carboxyl terminus of dystrophin, and dystroglycan has been shown to bind the extracellular matrix component laminin in a gel overlay assay (9,(14)(15)(16) gene (20, 24).In an effort to understand the genetic mutation responsible for SCARMD, we isolated and characterized cDNA and genomic sequences encoding human adhalin. To our surprise, the adhalin gene resides on chromosome 17q21, unlinked to the chromosome 13-encoded SCARMD locus. Additionally, a spli...

show abstract

Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24.

Cited by 128 publications

References 26 publications

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

Desmuslin, an intermediate filament protein that interacts with α-dystrobrevin and desmin

Human adhalin is alternatively spliced and the gene is located on chromosome 17q21.

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