Primary sequence and domain structure of chicken vinculin

Price, G J; Jones, Peter; Davison, Matt; Patel, Bipin; Bendori, R; Geiger, Benjamin; Critchley, David R.

doi:10.1042/bj2590453

Cited by 69 publications

(67 citation statements)

References 41 publications

(57 reference statements)

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“…Vinculin is strongly enriched in developing and adult smooth muscles as compared to other tissues. Metavinculin, a muscle-specific variant of the protein that appears as a result of alternative splicing of a single vinculin gene transcript (Price et al, 1989;Koteliansky et al, 1992), is a late marker of vascular smooth muscle. Meta-vinculin co-localizes with vinculin in dense plaques, the cell-extracellular matrix adherens junctions of smooth muscle cells (Belkin et al, 1988).…”

Section: Developmental Changes Of the Myoepithelial Cellsmentioning

confidence: 99%

Myoepithelial cell diffeentiation in the developing mammary gland: Progressive acquisition of smooth muscle phenotype

Deugnier

Moiseyeva

Thiery

et al. 1995

Developmental Dynamics

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The most important portion of the mammary gland development occurs postnatally, with distinct periods of intensive morphogenesis taking place between birth and puberty and during pregnancy and lactation. To characterize the differentiation process of mammary myoepithelial cells, we have studied the expression patterns of several smooth muscle phenotypic markers, including contractile proteins, a-smooth muscle-actin (a-SM-actin), smooth muscle myosin heavy chains (SM-MHC), and calponin; components of cell-extracellular matrix adherens junctions, phosphoglucomutase-related protein (PGM), vinculin variants, integrin subunits; and laminin variant chains in the developing rat mammary gland using immunofluorescence microscopy. a-SM-actin-and SM-MHC-positive cells were found first in newborn animals, while calponin, PGM and a1 integrin subunit began to be expressed in prepubertal animals (1.5 weeks). Vinculin, p1 and a3 integrin subunits were largely confined to the basal cell layer at all developmental stages examined with greater staining starting at 1.5 weeks. Meta-vinculin was identified only in myoepithelial cells of the lactating gland. yl laminin chain was present in the mammary gland basement membrane throughout development, while the p2 chain was revealed in 3-week-old animals and accumulated later in postpubertal animals (7 weeks). Similarly, p2 laminin chain was absent from the forming alveoli basement membrane in pregnant rats and started to accumulate in the lactating gland. In addition to temporal changes, we have observed spatial differences in the distribution of the phenotypic markers. Both in pre-and in postpubertal animals, a-SM-actinand SM-MHC-positive cells of the growing ductal ends contained low amounts if any of calponin, PGM, and p2 laminin chain. We conclude that during postnatal development, mammary myoepithelial cells progressively acquire a differentiated phenotype as revealed by the expression of various smooth muscle markers. Maturation of the myoepithelial cells is accompanied by upregulation of the smooth muscle integrin expression followed by accumulation of P2-containing laminin variant. Thus, changes in adhesion system parallel with the myoepithelial cell differentiation.D 1995 Wiley-Liss, Inc.

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Section: Developmental Changes Of the Myoepithelial Cellsmentioning

confidence: 99%

Myoepithelial cell diffeentiation in the developing mammary gland: Progressive acquisition of smooth muscle phenotype

Deugnier

Moiseyeva

Thiery

et al. 1995

Developmental Dynamics

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“…The two chick vinculin cDNAs used in this study (referred to as the 2.89-kb eDNA and cVinS) were both isolated from a chick embryo fibroblast Lgtll eDNA I~rary, and have been described elsewhere (Price et al, 1987(Price et al, , 1989Bendori et al, 1987).…”

Section: Vinculin Cdnasmentioning

confidence: 99%

Identification of a talin binding site in the cytoskeletal protein vinculin.

Jones

Jackson

Price

et al. 1989

The Journal of Cell Biology

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Abstract. Binding of the cytoskeletal protein vinculin to talin is one of a number of interactions involved in linking F-actin to cell-matrix junctions. To identify the talin binding domain in vinculin, we expressed the NH2-terminal region of the molecule encoded by two closely similar, but distinct vinculin cDNAs, using an in vitro transcription translation system. The 5' Eco RI-Bam HI fragment of a partial 2.89-kb vinculin cDNA encodes a 45-kD polypeptide containing the first 398 amino acids of the molecule. The equivalent restriction enzyme fragment of a second vinculin cDNA (cVin5) lacks nucleotides 746-867, and encodes a 41-kD polypeptide missing amino acids 167-207. The radiolabeled 45-kD vinculin polypeptide bound to microtiter wells coated with talin, but not BSA, and binding was inhibited by unlabeled vinculin. In contrast, the 41-kD vinculin polypeptide was devoid of talin binding activity. The role of residues 167-207 in talin binding was further analyzed by making a series of deletions spanning this region, each deletion of seven amino acids contiguous with the next.

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“…The fact that no amino acid difference could be observed between vinculin and meta-vinculin apart from this peptide suggested that they are encoded by alternatively spliced transcripts derived from a single gene [12]. Furthermore, extensive Southern-blot analysis of the human and chicken vinculin genes is consistent with a single functional gene [17,18] and the human vinculin gene has been mapped to chromosome 10q11.2-qter [18]. In the present communication, we establish that the human vinculin gene indeed contains an exon coding for the meta-vinculin-specific insert and that this exon is alternatively spliced giving rise to vinculin and metavinculin mRNA.…”

mentioning

confidence: 51%

“…The identity of vinculin and meta-vinculin sequences outside the meta-vinculin-specific insert region ([ 121 and this work) and the existence of a single gene in chicken [17] and human [18] suggests that meta-vinculin and vinculin mRNA species are generated by alternative splicing of vinculin premRNA. The partial genomic sequence presented here provides evidence for this mechanism.…”

Section: Discussionmentioning

confidence: 99%

“…The chicken meta-vinculin-specific DNA fragment was amplified via the polymerase-chain reaction using flanking oligonucleotide 1 (nucleotides 3020 -2992) and oligonucleotide 2 (nucleotides 2946 -2975) derived from the sequence of Price et al [17]. Prior to amplification, first-strand cDNA synthesis was carried out by reverse transcription of the mRNA using oligonucleotide 1 as the primer.…”

Section: Isolation Of Genomic Clonesmentioning

confidence: 99%

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An additional exon in the human vinculin gene specifically encodes meta‐vinculin‐specific difference peptide

Koteliansky

Ogryzko

Zhidkova

et al. 1992

European Journal of Biochemistry

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We have analyzed the structure, origin and expression of the high-molecular-mass muscle-specific variant of vinculin, called meta-vinculin. The meta-vinculin-specific inserts from the human and avian molecules have been isolated and sequenced and the sequences confirmed via cloning of the corresponding cDNA. Comparison of the human, avian and determined porcine sequences revealed cross-species identity in the C-terminal half of the insert. Human and porcine meta-vinculin were highly similar in the insert region, showing only five amino acid exchanges; avian meta-vinculin showed 22 exchanges in the same region compared to human meta-vinculin and exhibited, in addition, one extra amino acid, making 69 in all. Each insert was flanked by characteristic KWSSK motifs.Evidence for two vinculin mRNA species in human uterus smooth muscle was provided by reverse transcription combined with the polymerase chain reaction, as well as by ribonuclease-mapping analysis of cDNA/mRNA hybrids. One of the mRNA species contained an additional 204-nucleotide insert that precisely encoded the meta-vinculin-specific peptide.Sequence analysis of the appropriate portion of the human vinculin gene showed that the section coding for the meta-vinculin-specific insert is present as a discrete exon. Thus, meta-vinculin and vinculin mRNA are generated by alternative splicing.Vinculin is a 11 7-kDa cytoskeletal protein associated with membrane actin-filament-attachment sites of cell-cell and cellmatrix adherens-type junctions [I, 21. Several studies have shown a remarkable microheterogeneity of vinculin in the form of antigenically indistinguishable isoelectrophoretic variants, some of which show tissue-specific expression [3-51. In addition to iso-vinculins, smooth muscle and striated muscle contain an 150-kDa protein, denoted as meta-vinculin, which shares similar peptide-map patterns, antigenic and functional properties with vinculin [6-1 I]. Meta-vinculin and vinculin are localized in the same cellular adhesive structures, in microfilament-associated membrane-bound plaques of smooth muscle, in intercalated discs and costameres of cardiac muscle, and in focal contacts of cultivated smooth-muscle cells [ l l , 121. Recently it was established that meta-vinculin may serve as a specific marker of smooth muscle [lo, 13, 141; it was identified in all human, chicken and porcine smooth muscles but not in non-muscle tissues and cultured cells [lo, 13, 141. The expression of meta-vinculin in human aortic smooth- To obtain a more complete understanding of the structural relationship between vinculin and meta-vinculin, the amino acid sequence of a porcine meta-vinculin-specific peptide was determined 1121. Porcine vinculin and meta-vinculin differ by a 68-residue insert, located close to the C-terminal part of the molecule [12]. The fact that no amino acid difference could be observed between vinculin and meta-vinculin apart from this peptide suggested that they are encoded by alternatively spliced transcripts derived from a single gene [12]. Furtherm...

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Primary sequence and domain structure of chicken vinculin

Cited by 69 publications

References 41 publications

Myoepithelial cell diffeentiation in the developing mammary gland: Progressive acquisition of smooth muscle phenotype

Myoepithelial cell diffeentiation in the developing mammary gland: Progressive acquisition of smooth muscle phenotype

Identification of a talin binding site in the cytoskeletal protein vinculin.

An additional exon in the human vinculin gene specifically encodes meta‐vinculin‐specific difference peptide

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