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PMID: 2548572 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump.

Biochemistry ·Vol. 28 ·No. 10 ·1989-05-16 ·Pages 4253-8

James PH, Pruschy M, Vorherr TE, Penniston JT, Carafoli E

Abstract

The primary structure of a region of the erythrocyte plasma membrane calcium pump which is phosphorylated by the cAMP-dependent protein kinase has been determined. The sequence is A-P-T-K-R-N-S-S(P)-P-P-P-S-P-D. The site is located between the calmodulin binding domain and the C-terminus of the ATPase. The ATPase is phosphorylated only at this site by the cAMP-dependent protein kinase, and the phosphorylation is inhibited by calmodulin. The effect of the phosphorylation is to decrease the Km for Ca2+ of the purified ATPase from about 10 microM to about 1.4 microM and to increase the Vmax of ATP hydrolysis about 2-fold.

MeSH Terms
Amino Acid Sequence Binding Sites Calcium Channels/metabolism Cell Membrane/metabolism Cyclic AMP/metabolism Erythrocyte Membrane/metabolism Humans In Vitro Techniques Kinetics Molecular Sequence Data Molecular Structure Phosphorylation
Chemicals
Calcium Channels Cyclic AMP
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
James P H
Laboratory of Biochemistry, Swiss Federal Institute of Technology (ETH), Zurich, Switzerland.
Pruschy M
Vorherr T E
Penniston J T
Carafoli E
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1989-05-16
Pages
4253-8
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NIGMS NIH HHS · GM 28835 · United States
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