This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kaplan, J M Articles by Varmus, H E Search for Related Content PubMed PubMed Citation Articles by Kaplan, J M Articles by Varmus, H E

The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant.

Department of Microbiology, University of California, San Francisco 94143.

ABSTRACT

The transforming protein of Rous sarcoma virus, pp60v-src, is covalently coupled to myristic acid by an amide linkage to glycine 2. Myristylation promotes the association of pp60v-src with cellular membranes, and this subcellular location is essential for transforming activity. The findings presented here, in conjunction with the previous reports of others, imply that the seventh amino acid encoded by v-src might be important in the myristylation reaction. Replacement of lysine 7 by asparagine greatly reduced the myristylation, membrane association, and transforming activity of pp60v-src. In contrast, substitution of arginine at residue 7 had no effect on any of these properties of pp60v-src. Addition of amino acids 1 to 7 encoded by v-src was sufficient to cause myristylation of a src-pyruvate kinase fusion protein. We conclude that the recognition sequence for myristylation of pp60v-src comprises amino acids 1 to 7 and that lysine 7 is a critical component of this sequence.

This article has been cited by other articles:

• Tournaviti, S., Hannemann, S., Terjung, S., Kitzing, T. M., Stegmayer, C., Ritzerfeld, J., Walther, P., Grosse, R., Nickel, W., Fackler, O. T. (2007). SH4-domain-induced plasma membrane dynamization promotes bleb-associated cell motility. J. Cell Sci. 120: 3820-3829 [Abstract] [Full Text]  
• Perez, M., Greenwald, D. L., de La Torre, J. C. (2004). Myristoylation of the RING Finger Z Protein Is Essential for Arenavirus Budding. J. Virol. 78: 11443-11448 [Abstract] [Full Text]  
• Alonso, A., Narisawa, S., Bogetz, J., Tautz, L., Hadzic, R., Huynh, H., Williams, S., Gjorloff-Wingren, A., Bremer, M. C. D., Holsinger, L. J., Millan, J. L., Mustelin, T. (2004). VHY, a Novel Myristoylated Testis-restricted Dual Specificity Protein Phosphatase Related to VHX. J. Biol. Chem. 279: 32586-32591 [Abstract] [Full Text]  
• Liang, X., Lu, Y., Wilkes, M., Neubert, T. A., Resh, M. D. (2004). The N-terminal SH4 Region of the Src Family Kinase Fyn Is Modified by Methylation and Heterogeneous Fatty Acylation: ROLE IN MEMBRANE TARGETING, CELL ADHESION, AND SPREADING. J. Biol. Chem. 279: 8133-8139 [Abstract] [Full Text]  
• Mukherjee, A., Arnaud, L., Cooper, J. A. (2003). Lipid-dependent Recruitment of Neuronal Src to Lipid Rafts in the Brain. J. Biol. Chem. 278: 40806-40814 [Abstract] [Full Text]  
• Yipp, B. G., Robbins, S. M., Resek, M. E., Baruch, D. I., Looareesuwan, S., Ho, M. (2003). Src-family kinase signaling modulates the adhesion of Plasmodium falciparum on human microvascular endothelium under flow. Blood 101: 2850-2857 [Abstract] [Full Text]  
• Woods, D., Cherwinski, H., Venetsanakos, E., Bhat, A., Gysin, S., Humbert, M., Bray, P. F., Saylor, V. L., McMahon, M. (2001). Induction of {beta}3-Integrin Gene Expression by Sustained Activation of the Ras-Regulated Raf-MEK-Extracellular Signal-Regulated Kinase Signaling Pathway. Mol. Cell. Biol. 21: 3192-3205 [Abstract] [Full Text]  
• Yasuda, K., Kosugi, A., Hayashi, F., Saitoh, S.-i., Nagafuku, M., Mori, Y., Ogata, M., Hamaoka, T. (2000). Serine 6 of Lck Tyrosine Kinase: A Critical Site for Lck Myristoylation, Membrane Localization, and Function in T Lymphocytes. J. Immunol. 165: 3226-3231 [Abstract] [Full Text]  
• van't Hof, W., Resh, M. D. (1999). Dual Fatty Acylation of p59Fyn Is Required for Association with the T Cell Receptor zeta  Chain through Phosphotyrosine-Src Homology Domain-2 Interactions. J. Cell Biol. 145: 377-389 [Abstract] [Full Text]  
• Le Seyec, J., Chouteau, P., Cannie, I., Guguen-Guillouzo, C., Gripon, P. (1999). Infection Process of the Hepatitis B Virus Depends on the Presence of a Defined Sequence in the Pre-S1 Domain. J. Virol. 73: 2052-2057 [Abstract] [Full Text]  
• Aziz, N., Cherwinski, H., McMahon, M. (1999). Complementation of Defective Colony-Stimulating Factor 1 Receptor Signaling and Mitogenesis by Raf and v-Src. Mol. Cell. Biol. 19: 1101-1115 [Abstract] [Full Text]  
• Tognon, C. E., Kirk, H. E., Passmore, L. A., Whitehead, I. P., Der, C. J., Kay, R. J. (1998). Regulation of RasGRP via a Phorbol Ester-Responsive C1 Domain. Mol. Cell. Biol. 18: 6995-7008 [Abstract] [Full Text]  
• Li, S., Couet, J., Lisanti, M. P. (1996). Src Tyrosine Kinases, Galpha Subunits, and H-Ras Share a Common Membrane-anchored Scaffolding Protein, Caveolin. CAVEOLIN BINDING NEGATIVELY REGULATES THE AUTO-ACTIVATION OF Src TYROSINE KINASES. J. Biol. Chem. 271: 29182-29190 [Abstract] [Full Text]  
• Hu, Q., Davidson, D., Schwartzberg, P. L., Macchiarini, F., Lenardo, M. J., Bluestone, J. A., Matis, L. A. (1995). Identification of Rlk, a Novel Protein Tyrosine Kinase with Predominant Expression in the T Cell Lineage. J. Biol. Chem. 270: 1928-1934 [Abstract] [Full Text]  
• Abrams, C. S., Zhao, W. (1995). SH3 Domains Specifically Regulate Kinase Activity of Expressed Src Family Proteins. J. Biol. Chem. 270: 333-339 [Abstract] [Full Text]  
• Vincent, W S, Gregory, R J, Wadsworth, S C (1989). Embryonic expression of a Drosophila src gene: alternate forms of the protein are expressed in segmental stripes and in the nervous system.. Genes Dev. 3: 334-347 [Abstract]