Phosphorylation of the Na,K-ATPase alpha-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation.-Reference-Cited by-同舟云学术

Phosphorylation of the Na,K-ATPase alpha-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation.

Published:1994-09 Issue:39 Volume:269 Page:24437-24445
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Beguin P.,Beggah A.T.,Chibalin A.V.,Burgener-Kairuz P.,Jaisser F.,Mathews P.M.,Rossier B.C.,Cotecchia S.,Geering K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. The Na,K-ATPase: Structure-Function Relationship;Horisberger,1994

2. Sodium-dependent regulation of sodium, potassium-adenosine-tri-phosphatase (Na+, K+-ATPase) activity in medullary thick ascending limb of Henle segments. Effect of cyclic-adenosine-monophosphate guanosine-nucleotide-binding-protein activity and arginine vasopressin

3. Dopamine inhibits Na/K-ATPase in single tubules and cultured cells from distal nephron

4. Relationships between adenylate cyclase and Na+, K(+)-ATPase in rat pancreatic islets.

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