Agonist- and Protein Kinase C-Induced Phosphorylation Have Similar Functional Consequences for Gastrin-Releasing Peptide Receptor Signaling via Gq

2003 ◽  
Vol 64 (4) ◽  
pp. 890-904 ◽  
Author(s):  
Roxanne A. Ally ◽  
Kirk L. Ives ◽  
Elie Traube ◽  
Iman Eltounsi ◽  
Pei-Wen Chen ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Receptor Signaling ◽  
Peptide Receptor ◽  
Gastrin Releasing Peptide ◽  
Kinase C ◽  
Functional Consequences

scholarly journals Dual Regulation of the Parathyroid Hormone (PTH)/PTH-Related Peptide Receptor Signaling by Protein Kinase C and β-Arrestins

Endocrinology ◽  
2002 ◽  
Vol 143 (10) ◽  
pp. 3854-3865 ◽  
Author(s):  
Marián Castro ◽  
Frank Dicker ◽  
Jean-Pierre Vilardaga ◽  
Cornelius Krasel ◽  
Manfred Bernhardt ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Receptor Signaling ◽  
Peptide Receptor ◽  
Related Peptide ◽  
Kinase C

scholarly journals The Gastrin-releasing Peptide Receptor Is Rapidly Phosphorylated by a Kinase Other Than Protein Kinase C After Exposure to Agonist

1995 ◽  
Vol 270 (14) ◽  
pp. 8217-8224 ◽  
Author(s):  
Glenn S. Kroog ◽  
Eduardo Sainz ◽  
Peter J. Worland ◽  
Mark A. Akeson ◽  
Richard V. Benya ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peptide Receptor ◽  
Gastrin Releasing Peptide ◽  
Kinase C

RGSZ1 interacts with protein kinase C interacting protein PKCI-1 and modulates mu opioid receptor signaling

2007 ◽  
Vol 19 (4) ◽  
pp. 723-730 ◽  
Author(s):  
Seena K. Ajit ◽  
Suneela Ramineni ◽  
Wade Edris ◽  
Rachel A. Hunt ◽  
Wah-Tung Hum ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Opioid Receptor ◽  
Mu Opioid Receptor ◽  
Receptor Signaling ◽  
Interacting Protein ◽  
Mu Opioid ◽  
Kinase C

Radiolabelling of bovine myristoylated alanine-rich protein kinase C substrate (MARCKS) in an ADP-ribosylation reaction

1994 ◽  
Vol 72 (9-10) ◽  
pp. 391-396 ◽  
Author(s):  
D. Chao ◽  
D. L. Severson ◽  
H. Zwiers ◽  
M. D. Hollenberg
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Brain Homogenate ◽  
Bovine Brain ◽  
Two Dimensional Gel Electrophoresis ◽  
Adp Ribosylation ◽  
Substrate Protein ◽  
Kinase C ◽  
Neuronal Proteins ◽  
Functional Consequences

In an ADP-ribosylation reaction, we have observed the radiolabelling of a protein in a crude bovine brain homogenate, which upon two-dimensional gel electrophoresis migrated with an acidic pI (< 4.5) and an apparent molecular mass (80–90 kDa) consistent with the properties of the myristoylated, alanine-rich, protein kinase C substrate protein termed MARCKS. To establish the identity of this radiolabelled constituent in brain homogenates, we first purified bovine brain MARCKS using calmodulin-Sepharose affinity chromatography and we then supplemented the crude ADP-ribosylation reaction mixture with this purified MARCKS fraction. Concordant increases in radiolabelling and silver staining of the same protein component from the MARCKS-supplemented ADP-ribosylation reaction, as compared with the ADP-ribosylated crude homogenate, established the identity of this constituent as MARCKS. The radiolabelling of MARCKS was lower in comparison with the ADP-ribosylation of the related neuronal protein B-50/GAP-43 under identical reaction conditions. The potential functional consequences of the ADP-ribosylation of MARCKS are discussed and the possibility is raised that other members of the MARCKS family, such as the F52/MacMARCKS/MRP protein, may also be subject to ADP-ribosylation.Key words: MARCKS, ADP-ribosylation, neuronal proteins, B-50/GAP-43, kinase C, calmodulin.

Sign in / Sign up

Export Citation Format

Share Document