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Biochem Biophys Res Commun. 2009 Jan 23;378(4):732-7. doi: 10.1016/j.bbrc.2008.11.107. Epub 2008 Dec 4.

Rap2 function requires palmitoylation and recycling endosome localization.

Author information

1
Division of Cell Biology, Graduate School of Medicine, University of the Ryukyus, Okinawa, Japan.

Abstract

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.

PMID:
19061864
DOI:
10.1016/j.bbrc.2008.11.107
[Indexed for MEDLINE]

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