Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C.

Abstract:

:Lipocortin I is a 39-kilodalton membrane-associated protein that in A431 cells is phosphorylated on tyrosine in response to epidermal growth factor (EGF). We have used recombinant human lipocortin I as a substrate for several protein kinases and identified phosphorylated residues by a combination of peptide mapping and sequence analysis. Lipocortin I was phosphorylated near the amino terminus at Tyr-21 by recombinant pp60c-src. The same tyrosine residue was phosphorylated by polyoma middle T/pp60c-src complex, by recombinant pp50v-abl, and with A431 cell membranes by the EGF receptor/kinase. The primary site of phosphorylation by protein kinase C was also near the amino terminus at Ser-27. The major site of phosphorylation by adenosine cyclic 3',5'-phosphate dependent protein kinase was on the carboxy-terminal half of the molecule at Thr-216. These sites are compared to the phosphorylation sites previously located in the structurally related protein lipocortin II.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Varticovski L,Chahwala SB,Whitman M,Cantley L,Schindler D,Chow EP,Sinclair LK,Pepinsky RB

doi

10.1021/bi00410a024

subject

Has Abstract

pub_date

1988-05-17 00:00:00

pages

3682-90

issue

10

eissn

0006-2960

issn

1520-4995

journal_volume

27

pub_type

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