The Full-Length, Cytoplasmic C-Terminus of the β2-Adrenergic Receptor Expressed in E. coli Acts as a Substrate for Phosphorylation by Protein Kinase A, Insulin Receptor Tyrosine Kinase, GRK2, but Not Protein Kinase C and Suppresses Desensitization when Expressed in Vivo-Reference-Cited by-同舟云学术

The Full-Length, Cytoplasmic C-Terminus of the β2-Adrenergic Receptor Expressed in E. coli Acts as a Substrate for Phosphorylation by Protein Kinase A, Insulin Receptor Tyrosine Kinase, GRK2, but Not Protein Kinase C and Suppresses Desensitization when Expressed in Vivo

Published:2000-12 Issue:3 Volume:20 Page:451-461
ISSN:1046-5928
Container-title:Protein Expression and Purification
language:en
Short-container-title:Protein Expression and Purification

Author:

Doronin Sergey,Lin Fubao,Wang Hsien-yu,Malbon Craig C.

Publisher

Elsevier BV

Subject

Biotechnology

Reference38 articles.

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4. Beta-adrenergic receptor kinase: Identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor;Benovic;Proc. Natl. Acad. Sci. USA,1986

5. Removal of phosphorylation sites from the beta 2-adrenergic receptor delays onset of agonist-promoted desensitization;Bouvier;Nature,1988

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