TY - JOUR
T1 - Crosstalk between kinases and Nedd4 family ubiquitin ligases
AU - An, Heeseon
AU - Krist, David T.
AU - Statsyuk, Alexander V.
PY - 2014/7
Y1 - 2014/7
N2 - A dazzling array of human biological processes achieves coordination and balance through the posttranslational modification of protein residues with phosphate (95 Da) or ubiquitin (8565 Da). Over the past years, a reciprocal communication has become recognized between phosphorylating (kinases) and ubiquitinating (E3 ligases) enzymes. Such crosstalk occurs when a kinase acts on a ligase or vice versa to modify the catalytic activity, substrate specificity, or subcellular localization of the modified enzyme. In this review, we focus on the crosstalk between the nine members of the Nedd4 family E3 ubiquitin ligases with kinase signal transducers such as cell surface receptors, cytosolic kinases, phosphatases, and transcription factors. Since protein kinases are well explored and established therapeutic targets, we hypothesize that mapping E3 ligases onto kinase signalling networks will provide clues to the full therapeutic potential of pharmacologically targeting E3 ligases. This journal is
AB - A dazzling array of human biological processes achieves coordination and balance through the posttranslational modification of protein residues with phosphate (95 Da) or ubiquitin (8565 Da). Over the past years, a reciprocal communication has become recognized between phosphorylating (kinases) and ubiquitinating (E3 ligases) enzymes. Such crosstalk occurs when a kinase acts on a ligase or vice versa to modify the catalytic activity, substrate specificity, or subcellular localization of the modified enzyme. In this review, we focus on the crosstalk between the nine members of the Nedd4 family E3 ubiquitin ligases with kinase signal transducers such as cell surface receptors, cytosolic kinases, phosphatases, and transcription factors. Since protein kinases are well explored and established therapeutic targets, we hypothesize that mapping E3 ligases onto kinase signalling networks will provide clues to the full therapeutic potential of pharmacologically targeting E3 ligases. This journal is
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U2 - 10.1039/c3mb70572b
DO - 10.1039/c3mb70572b
M3 - Review article
C2 - 24457516
AN - SCOPUS:84901837668
SN - 1742-206X
VL - 10
SP - 1643
EP - 1657
JO - Molecular bioSystems
JF - Molecular bioSystems
IS - 7
ER -