Peptide mimetics of receptor extracellular domains modulate signal transduction by P2Y2 receptors

2006 ◽  
pp. 594-596
Author(s):  
Julia Brown ◽  
Colin A Brown ◽  
Ashley Martin ◽  
Ülo Langel ◽  
John Howl
Keyword(s):  
Signal Transduction ◽  
Peptide Mimetics ◽  
P2y2 Receptors ◽  
Extracellular Domains ◽  
Modulate Signal

scholarly journals Targeting of Protein Kinase Cα to Caveolae

1998 ◽  
Vol 141 (3) ◽  
pp. 601-610 ◽  
Author(s):  
Chieko Mineo ◽  
Yun-Shu Ying ◽  
Christine Chapline ◽  
Susan Jaken ◽  
Richard G.W. Anderson
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Regulatory Domain ◽  
Calcium Dependent ◽  
High Affinity ◽  
Membrane Invagination ◽  
Protein Kinase Cα ◽  
Flanking Sequences ◽  
Modulate Signal ◽  
Regulatory Functions

Previously, we showed caveolae contain a population of protein kinase Cα (PKCα) that appears to regulate membrane invagination. We now report that multiple PKC isoenzymes are enriched in caveolae of unstimulated fibroblasts. To understand the mechanism of PKC targeting, we prepared caveolae lacking PKCα and measured the interaction of recombinant PKCα with these membranes. PKCα bound with high affinity and specificity to caveolae membranes. Binding was calcium dependent, did not require the addition of factors that activate the enzyme, and involved the regulatory domain of the molecule. A 68-kD PKCα-binding protein identified as sdr (serum deprivation response) was isolated by interaction cloning and localized to caveolae. Antibodies against sdr inhibited PKCα binding. A 100–amino acid sequence from the middle of sdr competitively blocked PKCα binding while flanking sequences were inactive. Caveolae appear to be a membrane site where PKC enzymes are organized to carry out essential regulatory functions as well as to modulate signal transduction at the cell surface.

scholarly journals Cytoskeletal Active Drugs Modulate Signal Transduction in the Protein Kinase C Pathway.

1993 ◽  
Vol 18 (3) ◽  
pp. 151-160 ◽  
Author(s):  
Grace K. Pavlath ◽  
Yoshiko Shimizu ◽  
Nobuyoshi Shimizu
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Modulate Signal

scholarly journals Importance of extra- and intracellular domains of TLR1 and TLR2 in NFκB signaling

2003 ◽  
Vol 162 (6) ◽  
pp. 1099-1110 ◽  
Author(s):  
Frantisek Sandor ◽  
Eicke Latz ◽  
Fabio Re ◽  
Leisa Mandell ◽  
Galina Repik ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Confocal Microscopy ◽  
Cell Surface ◽  
Mononuclear Cells ◽  
Cytokine Secretion ◽  
Cross Linking ◽  
Toll Like Receptor ◽  
Extracellular Domains ◽  
Intracellular Domains ◽  
Simultaneous Expression

Recognition of ligands by toll-like receptor (TLR) 2 requires interactions with other TLRs. TLRs form a combinatorial repertoire to discriminate between the diverse microbial ligands. Diversity results from extracellular and intracellular interactions of different TLRs. This paper demonstrates that TLR1 and TLR2 are required for ara-lipoarabinomannan– and tripalmitoyl cysteinyl lipopeptide–stimulated cytokine secretion from mononuclear cells. Confocal microscopy revealed that TLR1 and TLR2 cotranslationally form heterodimeric complexes on the cell surface and in the cytosol. Simultaneous cross-linking of both receptors resulted in ligand-independent signal transduction. Using chimeric TLRs, we found that expression of the extracellular domains along with simultaneous expression of the intracellular domains of both TLRs was necessary to achieve functional signaling. The domains from each receptor did not need to be contained within a single contiguous protein. Chimeric TLR analysis further defined the toll/IL-1R domains as the area of crucial intracellular TLR1–TLR2 interaction.

Engineered GPCRs as Tools to Modulate Signal Transduction

Physiology ◽  
2008 ◽  
Vol 23 (6) ◽  
pp. 313-321 ◽  
Author(s):  
Ying Pei ◽  
Sarah C. Rogan ◽  
Feng Yan ◽  
Bryan L. Roth
Keyword(s):  
Signal Transduction ◽  
Signaling Pathways ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Designer Drugs ◽  
Modulate Signal ◽  
Synthetic Drug ◽  
G Protein Coupled

Different families of G-protein-coupled receptors (GPCRs) have been engineered to provide exclusive control over the activation of these receptors and thus to understand better the consequences of their signaling in vitro and in vivo. These engineered receptors, named RASSLs (receptors activated solely by synthetic ligands) and DREADDs (designer receptors exclusively activated by designer drugs), are insensitive to their endogenous ligands but can be activated by synthetic drug-like compounds. Currently, the existing RASSLs and DREADDs cover the Gi, Gq, and Gs signaling pathways. These modified GPCRs can be utilized as ideal tools to study GPCR functions selectively in specific cellular populations.

Heme-Edge Residues Modulate Signal Transduction within a Bifunctional Homo-Dimeric Sensor Protein

Biochemistry ◽  
2021 ◽  
Author(s):  
Dayna C. Patterson ◽  
Yilin Liu ◽  
Sayan Das ◽  
Neela H. Yennawar ◽  
Jean-Paul Armache ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Sensor Protein ◽  
Modulate Signal
Sign in / Sign up

Export Citation Format

Share Document