Abstract
Many cytokines transmit signals to the cell interior through activation of receptor-associated, Janus family protein tyrosine kinases (Jak PTKs). The interleukin-2 receptor (IL-2R) is associated with the Jak1 and Jak3 PTKs, and ligand-induced activation of these PTKs is essential for lymphocyte proliferation. Here, the nonreceptor PTK, Pyk2, was found to be activated following IL-2 stimulation in a Jak-dependent manner. Furthermore, physical association was detected between endogenous Pyk2 and Jak3, and a dominant interfering mutant of Pyk2 inhibited IL-2-induced cell proliferation without affecting Stat5 activation. Collectively, these results suggest that Pyk2 is a newly identified component of the Jak-mediated IL-2 signaling pathway.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Binding Sites / drug effects
-
Cell Division / drug effects
-
Cells, Cultured
-
DNA-Binding Proteins / drug effects
-
Enzyme Activation / drug effects
-
Focal Adhesion Kinase 2
-
Humans
-
Interleukin-2 / pharmacology
-
Janus Kinase 3
-
Milk Proteins*
-
Protein-Tyrosine Kinases / drug effects
-
Protein-Tyrosine Kinases / physiology*
-
Receptors, Interleukin-2 / drug effects
-
Receptors, Interleukin-2 / metabolism*
-
STAT5 Transcription Factor
-
Signal Transduction
-
Trans-Activators / drug effects
Substances
-
DNA-Binding Proteins
-
Interleukin-2
-
Milk Proteins
-
Receptors, Interleukin-2
-
STAT5 Transcription Factor
-
Trans-Activators
-
Protein-Tyrosine Kinases
-
Focal Adhesion Kinase 2
-
JAK3 protein, human
-
Janus Kinase 3