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In situ determination of a PKA phosphorylation site in the C-terminal region of filamin.
Jay, David; García, Elizabeth J; de la Luz Ibarra, María.
Afiliação
  • Jay D; Departamento de Biomedicina Molecular Cardiovascular, Instituto Nacional de Cardiología, Ignacio Chávez, Mexico City, Mexico. jay@sin.conacyt.mx
Mol Cell Biochem ; 260(1-2): 49-53, 2004 May.
Article em En | MEDLINE | ID: mdl-15228085
A C-terminal region of human endothelial actin-binding protein-280 (ABP-280 or ABP, non-muscle filamin) was subcloned and efficiently expressed in a mammalian cells system as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting analysis. As predicted by the aminoacid sequence, the fragment, a 79 kD peptide (residues 1671-2361, plus 3.9 kD from an N-terminal fusion peptide included in the expression plasmid), contained the two potential cAMP-dependent protein kinase (PKA) phosphorylation sites (serine 2152 and threonine 2336) predicted to be present in this region of the molecule. Incubation of cells in the presence of cAMP-elevating agents enhanced 32P uptake into the fragment. Site-directed mutagenesis analysis indicated that serine 2152 is the unique substrate in the C-terminal region of ABP for endogenously activated PKA. The functional implications of phosphorylation of this residue, which belongs to a serine-proline motif, are discussed in terms of the role of filamin in cytoskeleton reorganization.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Proteínas Contráteis / Proteínas dos Microfilamentos Limite: Humans Idioma: En Revista: Mol Cell Biochem Ano de publicação: 2004 Tipo de documento: Article País de afiliação: México País de publicação: Holanda
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Proteínas Contráteis / Proteínas dos Microfilamentos Limite: Humans Idioma: En Revista: Mol Cell Biochem Ano de publicação: 2004 Tipo de documento: Article País de afiliação: México País de publicação: Holanda