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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-6-5
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pubmed:abstractText |
Three different C-terminal regions of human endothelial actin-binding protein-280 (ABP-280 or ABP; nonmuscle filamin) were subcloned and efficiently expressed in the Escherichia coli BL21 (DE3) system as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. As predicted by the aminoacid sequence one of the fragments, a 109-kDa peptide (residues 1671-2647), contained a calpain cleavage site and two potential cAMP-dependent protein kinase (PKA) phosphorylation sites (serine 2152 and threonine 2336). A second fragment, a 74-kDa peptide (residues 1671-2331), contained a calpain cleavage site and one of the three presumptive PKA phosphorylation sites (serine 2152). The third fragment, a 48-kDa peptide (residues 2223-2647), contained only one of the PKA sites (threonine 2336). Phosphorylation of these truncated peptides indicated that only the fragments containing serine 2152 incorporated phosphate after PKA treatment. Site-directed mutagenesis analysis confirmed that serine 2152 is the unique substrate for PKA in the C-terminal region of ABP. The functional significance of phosphorylation of this residue, which belongs to a serine-proline motif, is discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Contractile Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/filamins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
377
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
80-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10775444-Amino Acid Motifs,
pubmed-meshheading:10775444-Amino Acid Substitution,
pubmed-meshheading:10775444-Blood Platelets,
pubmed-meshheading:10775444-Calpain,
pubmed-meshheading:10775444-Contractile Proteins,
pubmed-meshheading:10775444-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:10775444-Endothelium,
pubmed-meshheading:10775444-Humans,
pubmed-meshheading:10775444-Immune Sera,
pubmed-meshheading:10775444-Microfilament Proteins,
pubmed-meshheading:10775444-Molecular Weight,
pubmed-meshheading:10775444-Mutation,
pubmed-meshheading:10775444-Peptide Fragments,
pubmed-meshheading:10775444-Phosphorylation,
pubmed-meshheading:10775444-Phosphoserine,
pubmed-meshheading:10775444-Recombinant Proteins,
pubmed-meshheading:10775444-Sequence Analysis, Protein,
pubmed-meshheading:10775444-Serine,
pubmed-meshheading:10775444-Threonine
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pubmed:year |
2000
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pubmed:articleTitle |
Determination of a cAMP-dependent protein kinase phosphorylation site in the C-terminal region of human endothelial actin-binding protein.
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pubmed:affiliation |
Departamento de Cultivo de Tejidos, Instituto Nacional de Cardiología, Ignacio Chávez, Juan Badiano #1, D. F. México. jay@mailer.main.conacyt.mx
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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