Abstract:
:The activated mutants of the α-subunits of G proteins G(12) and G(13) have been designated as the gep oncogenes owing to their ability to stimulate diverse oncogenic signaling pathways that lead to neoplastic transformation of fibroblast cell lines and tumorigenesis in nude mice models. Studies from our laboratory as well as others have shown that the growth-promoting activities of Gα(12) and Gα(13) involve potent activation of c-Jun N-terminal kinases (JNKs). Our previous studies have indicated that the JNK-interacting leucine zipper protein (JLP), a scaffold protein involved in the structural and functional organization of the JNK/p38 mitogen-activated protein kinase module, tethers Gα(12) and Gα(13) to the JNK signaling module. In the present study, in addition to demonstrating the physical association between JLP and Gα(12), we show that this interaction is enhanced by the receptor- or mutation-mediated activation of Gα(12). We also establish that JLP interacts with Gα(12) through the C-terminal domain that has been previously identified to be involved in binding to Gα(13). Furthermore, using this C-terminal domain as a competitively inhibitor of JLP that can disrupt Gα(12)-JLP interaction, we demonstrate that JLP is required for the stimulation of JNK by Gα(12). Our results also indicate that such JLP interaction is required for Gα(12) as well as Gα(13)-mediated neoplastic transformation of JLP. These studies demonstrate for the first time a functional role for JLP in the gep oncogene-regulated neoplastic signaling pathway.
journal_name
Neoplasiajournal_title
Neoplasia (New York, N.Y.)authors
Kashef K,Radhakrishnan R,Lee CM,Reddy EP,Dhanasekaran DNdoi
10.1593/neo.101622subject
Has Abstractpub_date
2011-04-01 00:00:00pages
358-64issue
4eissn
1522-8002issn
1476-5586journal_volume
13pub_type
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