First Author | Uechi Y | Year | 2009 |
Journal | Biochem Biophys Res Commun | Volume | 378 |
Issue | 4 | Pages | 732-7 |
PubMed ID | 19061864 | Mgi Jnum | J:142909 |
Mgi Id | MGI:3822406 | Doi | 10.1016/j.bbrc.2008.11.107 |
Citation | Uechi Y, et al. (2009) Rap2 function requires palmitoylation and recycling endosome localization. Biochem Biophys Res Commun 378(4):732-7 |
abstractText | Rap2A, Rap2B, and Rap2C are Ras-like small G proteins. The role of their post-translational processing has not been investigated due to the lack of information on their downstream signaling. We have recently identified the Traf2- and Nck-interacting kinase (TNIK), a member of the STE20 group of mitogen-activated protein kinase kinase kinase kinases, as a specific Rap2 effector. Here we report that, in HEK293T cells, Rap2A (farnesylated) and Rap2C (likely farnesylated), but not Rap2B (geranylgeranylated), require palmitoylation for membrane-association and TNIK activation, whereas all Rap2 proteins, including Rap2B, require palmitoylation for induction of TNIK-mediated phenotype, the suppression of cell spreading. Furthermore, we report for the first time that, in COS-1 cells, Rap2 proteins localize, and recruit TNIK, to the recycling endosomes, but not the Golgi nor the endoplasmic reticulum, in a palmitoylation-dependent manner. These observations implicate the involvement of palmitoylation and recycling endosome localization in cellular functions of Rap2 proteins. |