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DHHC9 and GCP16 Constitute a Human Protein Fatty Acyltransferase with Specificity for H- and N-Ras
Open accessAbstract
Covalent lipid modifications mediate the membrane attachment and biological activity of Ras proteins. All Ras isoforms are farnesylated and carboxyl-methylated at the terminal cysteine; H-Ras and N-Ras are further modified by palmitoylation. Yeast Ras is palmitoylated by the DHHC cysteine-rich domain-containing protein Erf2 in a complex with Erf4. Here we report that H- and N-Ras are palmitoylated by a human protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes. DHHC9 is an integral membrane protein that contains a DHHC cysteine-rich domain. GCP16 encodes a Golgi-localized membrane protein that has limited sequence similarity to yeast Erf4. DHHC9 and GCP16 co-distribute in the Golgi apparatus, a location consistent with the site of mammalian Ras palmitoylation in vivo. Like yeast Erf2.Erf4, DHHC9 and GCP16 form a protein complex, and DHHC9 requires GCP16 for protein fatty acyltransferase activity and protein stability. Purified DHHC9.GCP16 exhibits substrate specificity, palmitoylating H- and N-Ras but not myristoylated G (alphai1) or GAP-43, proteins with N-terminal palmitoylation motifs. Hence, DHHC9.GCP16 displays the properties of a functional human ortholog of the yeast Ras palmitoyltransferase.
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Cites
Ras signalling on the endoplasmic reticulum and the Golgi
Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., Cox, A. D., & Philips, M. R. (2002) · Nature Cell Biology · doi:10.1038/ncb783 · Cited by 594
PROTEIN PRENYLATION: GENES, ENZYMES, TARGETS, AND FUNCTIONS
Schafer, W. R., & Rine, J. (1992) · Annual Review of Genetics · doi:10.1146/annurev.ge.26.120192.001233 · Cited by 377
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RAS Proteins and Their Regulators in Human Disease
Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943
Drugging the undruggable RAS: Mission Possible?
Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997
Wang, T., Yu, H., Hughes, N. W., Liu, B., Kendirli, A., Klein, K., Chen, W. W., Lander, E. S., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.01.013 · Cited by 632
Global Analysis of Protein Palmitoylation in Yeast
Roth, A. F., Wan, J., Bailey, A. O., Sun, B., Kuchar, J. A., Green, W. N., Phinney, B. S., Yates, J. R., & Davis, N. G. (2006) · Cell · doi:10.1016/j.cell.2006.03.042 · Cited by 543
The Palmitoylation Machinery Is a Spatially Organizing System for Peripheral Membrane Proteins
Rocks, O., Gerauer, M., Vartak, N., Koch, S., Huang, Z.-P., Pechlivanis, M., Kuhlmann, J., Brunsveld, L., Chandra, A., Ellinger, B., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.007 · Cited by 454
Metadata
- Authors
- Swarthout, J. T., Lobo, S., Farh, L., Croke, M. R., Greentree, W. K., Deschenes, R. J., & Linder, M. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-09
- Volume
- 280
- Issue
- 35
- Pages
- 31141-31148
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2018925580
- Cited by
- 354
- References
- 2
- FWCI
- 6.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Swarthout, J. T., Lobo, S., Farh, L., Croke, M. R., Greentree, W. K., Deschenes, R. J., & Linder, M. E. (2005). DHHC9 and GCP16 Constitute a Human Protein Fatty Acyltransferase with Specificity for H- and N-Ras. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m504113200
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