The 38-Amino-Acid Form of Pituitary Adenylate Cyclase-Activating Polypeptide Induces Neurite Outgrowth in PC12 Cells that Is Dependent on Protein Kinase C and Extracellular Signal-Regulated Kinase but not on Protein Kinase A, Nerve Growth Factor Receptor Tyrosine Kinase, p21rasG protein, and pp60c-srcCytoplasmic Tyrosine Kinase

1998 ◽  
Vol 54 (3) ◽  
pp. 547-558 ◽  
Author(s):  
Philip Lazarovici ◽  
Hao Jiang ◽  
Donald Fink
Keyword(s):  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Growth Factor Receptor ◽  
Acid Form ◽  
Extracellular Signal Regulated Kinase ◽  
Kinase C ◽  
Extracellular Signal ◽  
Pituitary Adenylate Cyclase ◽  
Amino Acid Form

The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in mast cells

Blood ◽  
2010 ◽  
Vol 115 (19) ◽  
pp. 3899-3906 ◽  
Author(s):  
Sebastian Drube ◽  
Sylvia Heink ◽  
Sabine Walter ◽  
Tobias Löhn ◽  
Mandy Grusser ◽  
...  
Keyword(s):  
Mast Cells ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Interleukin 1 ◽  
Structural Basis ◽  
Extracellular Signal Regulated Kinase ◽  
Kit Ligand ◽  
Kinase C ◽  
Extracellular Signal ◽  
Transcription 3

Abstract Members of the Toll/interleukin-1 receptor (TIR) family are of importance for host defense and inflammation. Here we report that the TIR-family member interleukin-33R (IL-33R) cross-activates the receptor tyrosine kinase c-Kit in human and murine mast cells. The IL-33R–induced activation of signal transducer and activator of transcription 3 (STAT3), extracellular signal-regulated kinase 1/2 (Erk1/2), protein kinase B (PKB), and Jun NH2-terminal kinase 1 (JNK1) depends on c-Kit and is required to elicit optimal effector functions. Costimulation with the c-Kit ligand stem cell factor (SCF) is necessary for IL-33–induced cytokine production in primary mast cells. The structural basis for this cross-activation is the complex formation between c-Kit, IL-33R, and IL-1R accessory protein (IL-1RAcP). We found that c-Kit and IL-1RAcP interact constitutively and that IL-33R joins this complex upon ligand binding. Our findings support a model in which signals from seemingly disparate receptors are integrated for full cellular responses.

scholarly journals Glucose Activates Protein Kinase C-ζ/λ through Proline-rich Tyrosine Kinase-2, Extracellular Signal-regulated Kinase, and Phospholipase D

2001 ◽  
Vol 276 (38) ◽  
pp. 35537-35545 ◽  
Author(s):  
Gautam Bandyopadhyay ◽  
Mini P. Sajan ◽  
Yoshinori Kanoh ◽  
Mary L. Standaert ◽  
Michael J. Quon ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Phospholipase D ◽  
Extracellular Signal Regulated Kinase ◽  
Kinase C ◽  
Tyrosine Kinase 2 ◽  
Extracellular Signal
Sign in / Sign up

Export Citation Format

Share Document