c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).
Synonyms: MAPK8IP2, C jun amino terminal kinase interacting protein 2, C-jun-amino-terminal kinase-interacting protein 2, Homologous to mouse JIP 1, IB 2, IB-2, IB2, Islet brain 2, Islet-brain-2, JIP 2, JIP-2, JIP2, JIP2_HUMAN, JNK interacting protein 2, JNK MAP kinase scaffold protein 2, JNK MAP kinase scaffold protein JIP2, JNK-interacting protein 2, MAPK8IP2, Mitogen activated protein kinase 8 interacting protein 2, Mitogen-activated protein kinase 8-interacting protein 2, PRKM8 interacting protein like, PRKM8IPL.