Ar. Ramjaun et al., Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase, J BIOL CHEM, 276(31), 2001, pp. 28913-28919
The endophilin family of proteins function in clathrin-mediated endocytosis
. Here, we have identified and cloned the rat germinal center kinase-like k
inase (rGLK), a member of the GCK (germinal center kinase) family of e-Jun
N-terminal kinase (JNK) activating enzymes, as a novel endophilin I-binding
partner. The interaction occurs both in vitro and in cells and is mediated
by the Src homology 3 domain of endophilin I and a region of rGLK containi
ng the endophilin consensus-binding sequence PPRPPPPR. Overlay analysis of
rat brain extracts demonstrates that endophilin I is a major Src homology 3
domain-binding partner for rGLK. Overexpression of full-length endophilin
I activates rGLK-mediated JNK activation, whereas N- and C-terminal fragmen
ts of endophilin I block JNK activation. Thus, endophilin I appears to have
a novel function in JNK activation.