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- W2003040903 endingPage "2688" @default.
- W2003040903 startingPage "2681" @default.
- W2003040903 abstract "A variety of immunoregulatory signals to effector T cells from monocytes, macrophages and regulatory T cells act through cyclic adenosine monophosphate. In the effector T cell, the protein kinase A (PKA) type I isoenzyme localizes to lipid rafts during T cell activation and modulates directly the proximal events that take place after engagement of the T cell receptor. The most proximal target for PKA phosphorylation is C‐terminal Src kinase (Csk), which initiates a negative signal pathway that fine‐tunes the T cell activation process. The A kinase anchoring protein Ezrin colocalizes PKA and Csk by forming a supramolecular signaling complex consisting of PKA, Ezrin, Ezrin/radixin/moesin (ERM) binding protein of 50 kDa (EBP50), phosphoprotein associated with glycosphingolipid‐enriched membrane microdomains (GEMs) (PAG) and Csk." @default.
- W2003040903 created "2016-06-24" @default.
- W2003040903 creator A5039702458 @default.
- W2003040903 creator A5042862730 @default.
- W2003040903 date "2010-04-24" @default.
- W2003040903 modified "2023-09-25" @default.
- W2003040903 title "Spatiotemporal control of cyclic AMP immunomodulation through the PKA-Csk inhibitory pathway is achieved by anchoring to an Ezrin-EBP50-PAG scaffold in effector T cells" @default.
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