RESUMO
The full length cDNA of porcine moesin and radixin have been cloned and sequenced. Comparison of the closely related sequences of human, murine and porcine moesin, ezrin and radixin with a protein from Echinococcus multilocularis, an evolutionarily quite distant human parasite, reveals several highly invariant domains in the aminoterminal and carboxyterminal regions. Most of these conserved domains are clustered around tyrosine residues that are putative phosphorylation sites for tyrosine phosphokinases.
Assuntos
Proteínas Sanguíneas/genética , Sequência Conservada , Proteínas do Citoesqueleto , Proteínas de Membrana/genética , Proteínas dos Microfilamentos , Proteínas/genética , Suínos/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Proteínas Sanguíneas/biossíntese , Proteínas Sanguíneas/química , Clonagem Molecular , DNA Complementar/química , DNA Complementar/metabolismo , Echinococcus/genética , Humanos , Proteínas de Membrana/biossíntese , Proteínas de Membrana/química , Camundongos , Dados de Sequência Molecular , Fosfoproteínas/química , Fosfoproteínas/genética , Biossíntese de Proteínas , Proteínas/química , Homologia de Sequência de AminoácidosRESUMO
Moesin (membrane-organizing extension spike protein, pronounced mó ez in) has previously been isolated from bovine uterus and characterized as a possible receptor protein for heparan sulfate. We now have cloned and sequenced its complete cDNA, which represents a single 4.2-kilobase mRNA encoding a protein of 577 amino acids. It contains no apparent signal peptide or transmembrane domain. In addition, the protein shows significant sequence identity (72%) to ezrin (cytovillin, p81), as well as similarity to protein 4.1 and talin. All of the latter proteins have been postulated to serve as structural links between the plasma membrane and the cytoskeleton. A similar role for moesin is implied by structure and domain predictions derived from the cDNA-deduced peptide sequence. Furthermore, our data indicate that moesin is identical to the 77-kDa band that copurifies with ezrin in its isolation from human placenta [Bretscher, A. (1989) J. Cell Biol. 108, 921-930].
Assuntos
Proteínas dos Microfilamentos , Proteínas/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Northern Blotting , Western Blotting , Bovinos , Clonagem Molecular , Proteínas do Citoesqueleto , Citoesqueleto/ultraestrutura , Expressão Gênica , Humanos , Dados de Sequência Molecular , Fosfoproteínas/química , Biossíntese de Proteínas , Conformação Proteica , Proteínas/química , RNA Mensageiro/genética , Mapeamento por Restrição , Alinhamento de Sequência , Talina/químicaRESUMO
Moesin is a member of a recently discovered family of closely related proteins that includes ezrin, radixin, and merlin. It is widely expressed in different tissues and cells and has been localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and cell movement. Here, we have localized the coding gene (MSN) to Xq11.2-q12 by Southern and Western blot analyses of Chinese hamster x human somatic cell hybrids and by fluorescence chromosomal in situ hybridization. Moesin-like sequences were identified on chromosomes 5 and 6. The murine Msn locus was mapped to the X chromosome as well by studying a rodent x mouse hybrid panel. The structure of the human moesin gene has been determined. The 12 exons are distributed over > 30 kb, and the exon/intron junctions demarcate individual highly conserved domains. Primer extension analysis revealed two major start transcription sites, 184 and 133 bp upstream of the initiation codon. The 5'-flanking region is GC-rich, lacks a TATA box, and contains four SP1 and one AP1 binding sites.