scholarly journals Translocation of Diacylglycerol Kinase θ from Cytosol to Plasma Membrane in Response to Activation of G Protein-coupled Receptors and Protein Kinase C

2005 ◽  
Vol 280 (11) ◽  
pp. 9870-9878 ◽  
Author(s):  
Jürgen van Baal ◽  
John de Widt ◽  
Nullin Divecha ◽  
Wim J. van Blitterswijk
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein ◽  
Diacylglycerol Kinase ◽  
G Protein Coupled Receptors ◽  
Kinase C ◽  
G Protein Coupled

G-protein-coupled receptors act via protein kinase C and Src to regulate NMDA receptors

10.1038/7243 ◽  
1999 ◽  
Vol 2 (4) ◽  
pp. 331-338 ◽  
Author(s):  
W-Y. Lu ◽  
Z-G. Xiong ◽  
S. Lei ◽  
B. A. Orser ◽  
E. Dudek ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nmda Receptors ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Kinase C ◽  
G Protein Coupled

Multiple Signaling Pathways for Platelet-Activating Factor Receptor

Physiology ◽  
1992 ◽  
Vol 7 (2) ◽  
pp. 72-75
Author(s):  
SD Shukla
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Signaling Pathways ◽  
G Protein ◽  
Platelet Activating Factor ◽  
G Protein Coupled Receptors ◽  
Kinase C ◽  
Paf Receptor ◽  
Multiple Signaling ◽  
G Protein Coupled

Platelet-activating factor (PAF) receptor is coupled to multiple signaling pathways, including phospholipid turnover via phospholipases C, D, A2;Ca2+ mobilization;and activation of protein kinase C and tyrosine kinase. The cloned receptor shows homology to G protein-coupled receptors. These developments highlight receptor functions of this novel phospholipid agonist.

scholarly journals Dynamic Regulation of Mammalian Numb by G Protein-coupled Receptors and Protein Kinase C Activation: Structural Determinants of Numb Association with the Cortical Membrane

2006 ◽  
Vol 17 (9) ◽  
pp. 4142-4155 ◽  
Author(s):  
Sascha E. Dho ◽  
JoAnn Trejo ◽  
David P. Siderovski ◽  
C. Jane McGlade
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein Coupled Receptors ◽  
Structural Determinants ◽  
Binding Motifs ◽  
Kinase C ◽  
G Protein Coupled ◽  
Pkc Activation ◽  
Ptb Domain

The cell fate determinant Numb is a membrane-associated adaptor protein involved in both development and intracellular vesicular trafficking. It has a phosphotyrosine-binding (PTB) domain and COOH-terminal endocytic-binding motifs for α-adaptin and Eps15 homology domain-containing proteins. Four isoforms of Numb are expressed in vertebrates, two of which selectively associate with the cortical membrane. In this study, we have characterized a cortical pool of Numb that colocalizes with AP2 and Eps15 at substratum plasma membrane punctae and cortical membrane-associated vesicles. Green fluorescent protein (GFP)-tagged mutants of Numb were used to identify the structural determinants required for localization. In addition to the previously described association of the PTB domain with the plasma membrane, we show that the AP2-binding motifs facilitate the association of Numb with cortical membrane punctae and vesicles. We also show that agonist stimulation of G protein-coupled receptors (GPCRs) that are linked to phospholipase Cβ and protein kinase C (PKC) activation causes redistribution of Numb from the cortical membrane to the cytosol. This effect is correlated with Numb phosphorylation and an increase in its Triton X-100 solubility. Live-imaging analysis of mutants identified two regions within Numb that are independently responsive to GPCR-mediated lipid hydrolysis and PKC activation: the PTB domain and a region encompassing at least three putative PKC phosphorylation sites. Our data indicate that membrane localization of Numb is dynamically regulated by GPCR-activated phospholipid hydrolysis and PKC-dependent phosphorylation events.

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