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- W2043912325 abstract "Scaffolding proteins play a critical role in conferring specificity and fidelity to signaling pathways. The JNK-interacting leucine zipper protein (JLP) has been identified as a scaffolding protein involved in linking components of the JNK signaling module. Gα12 and Gα13, the α-subunits of heterotrimeric G proteins G12 and G13, respectively, stimulate the JNK module in diverse cell types. Here, we report that Gα13 physically interacts with JLP, and this interaction enhances Gα13-mediated JNK activation. We also demonstrate endogenous interaction between JLP and Gα13 in MCF-7 cells. JLP interaction is specific to the G12 family of α-subunits via its C-terminal domain (termed GID-JLP), spanning amino acids 1165−1307, and this interaction is more pronounced with the mutationally or functionally activated form of Gα13 compared to that of wild-type Gα13. The presence of a ternary complex consisting of Gα13, JLP, and JNK suggests a role for JLP in tethering Gα13 to the signaling components involved in JNK activation. Coexpression of GID-JLP disrupts ternary complex formation in addition to attenuating Gα13-stimulated JNK activity. These findings identify JLP as a novel scaffolding protein in the Gα13-mediated JNK signaling pathway." @default.
- W2043912325 created "2016-06-24" @default.
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- W2043912325 date "2005-10-01" @default.
- W2043912325 modified "2023-10-17" @default.
- W2043912325 title "JNK-Interacting Leucine Zipper Protein Is a Novel Scaffolding Protein in the Gα<sub>13</sub> Signaling Pathway" @default.
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- W2043912325 doi "https://doi.org/10.1021/bi050604l" @default.
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