Premium
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
Author(s) -
Cornez Isabelle,
Taskén Kjetil
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.056
Subject(s) - ezrin , moesin , microbiology and biotechnology , radixin , scaffold protein , protein kinase a , tyrosine protein kinase csk , phosphoprotein , effector , chemistry , kinase , signal transduction , phosphorylation , biology , biochemistry , proto oncogene tyrosine protein kinase src , cell , cytoskeleton , sh3 domain
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.