Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M111.254599
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dc.titlePrenylated C17orf37 induces filopodia formation to promote cell migration and metastasis
dc.contributor.authorDasgupta, S.
dc.contributor.authorCushman, I.
dc.contributor.authorKpetemey, M.
dc.contributor.authorCasey, P.J.
dc.contributor.authorVishwanatha, J.K.
dc.date.accessioned2014-11-26T08:29:59Z
dc.date.available2014-11-26T08:29:59Z
dc.date.issued2011-07-22
dc.identifier.citationDasgupta, S., Cushman, I., Kpetemey, M., Casey, P.J., Vishwanatha, J.K. (2011-07-22). Prenylated C17orf37 induces filopodia formation to promote cell migration and metastasis. Journal of Biological Chemistry 286 (29) : 25935-25946. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M111.254599
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/110225
dc.description.abstractPost-translational modification by covalent attachment of isoprenoid lipids (prenylation) regulates the functions and biological activities of several proteins implicated in the oncogenic transformation and metastatic progression of cancer. The largest group of prenylated proteins contains a CAAX motif at the C-terminal that serves as a substrate for a series of post-translational modifications that convert these otherwise hydrophilic proteins to lipidated proteins, thus facilitating membrane association. C17orf37 (chromosome 17 open reading frame 37), also known as C35/Rdx12/MGC14832, located in the 17q12 amplicon, is overexpressed in human cancer, and its expression correlates with the migratory and invasive phenotype of cancer cells. Here we show that C17orf37 contains a functional CAAX motif and is post-translationally modified by protein geranylgeranyltransferase-I (GGTase-I). Geranylgeranylation of C17orf37 at the CAAX motif facilitates association of the protein to the inner leaflet of plasma membrane, enhances migratory phenotype of cells by inducing increased filopodia formation, and potentiates directional migration. A prenylation-deficient mutant of C17orf37 is functionally inactive and fails to trigger dissemination of tail vein-injected cells in a mouse model of metastasis. These findings demonstrate that prenylation is required for the function of the C17orf37 protein in cancer cells and imply that the post-translational modification may functionally regulate metastatic progression of disease. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M111.254599
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentDUKE-NUS GRADUATE MEDICAL SCHOOL S'PORE
dc.description.doi10.1074/jbc.M111.254599
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume286
dc.description.issue29
dc.description.page25935-25946
dc.description.codenJBCHA
dc.identifier.isiut000293073000053
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