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Phosphorylation of p36 in vitro with pp60 src
Author(s) -
Glenney John R.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80047-8
Subject(s) - phosphatidylserine , phosphorylation , chemistry , kinase , in vitro , protein phosphorylation , proto oncogene tyrosine protein kinase src , microbiology and biotechnology , tyrosine phosphorylation , substrate level phosphorylation , phospholipid , biochemistry , protein kinase a , biology , membrane
P36 is a major substrate of the tyrosine protein kinases. P36 isolated from bovine intestine was used in phosphorylation reactions with pp60 src . Phosphorylation was stimulated 3–5‐fold by Ca 2+ , however the K m was the same (2.5μM) at high or low Ca 2+ . Although the level of free Ca 2+ needed for this enhanced phosphorylation was 10 −4 –10 −3 ) −3 M, phosphatidylserine shifted the Ca 2+ sensitivity to the 10 −6 –10 −5 M range. Independent evidence suggested that p36 interacts directly with liposomes containing phosphatidylserine. This raises the possibility that p36, like c‐kinase, is a Ca 2+ ‐activated, phospholipid‐dependent protein.