Characterization of sites of serine phosphorylation in human placental insulin receptor copurified with insulin-stimulated serine kinase activity by two-dimensional thin-layer peptide mapping

Insulin receptor was copurified from human placenta together with insulin-stimulated kinase activity that phosphorylates the insulin receptor on serine residues. Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phos...

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Bibliographic Details
Published in:FEBS letters 1989-01, Vol.242 (2), p.301-304
Main Authors: Smith, David M., Sale, Graham J.
Format: Article
Language:English
Subjects:
Humans
Insulin
Peptide Mapping
Phosphorylation
Phosphoserine - metabolism
Phosphotyrosine
placenta
Placenta - metabolism
Protein Kinases - isolation & purification
Protein Kinases - metabolism
Protein phosphorylation
Protein-Serine-Threonine Kinases
Receptor
Receptor, Insulin - isolation & purification
Receptor, Insulin - metabolism
serine
Serine - analogs & derivatives
Serine kinase
Tyrosine - analogs & derivatives
Tyrosine - metabolism
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Summary:Insulin receptor was copurified from human placenta together with insulin-stimulated kinase activity that phosphorylates the insulin receptor on serine residues. Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phosphorylation in the insulin receptor were recovered in the same peptides as those known to be phosphorylated on serine in vivo in response to insulin. This indicates that the serine kinase copurified with the insulin receptor represents a physiologically important enzyme involved in the insulin triggered serine phosphorylation of the insulin receptor in vivo.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)80489-2