Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 29 January 1993:
Vol. 259. no. 5095, pp. 683 - 686
DOI: 10.1126/science.8430318
Prev | Table of Contents | Next

Articles

Science, Vol 259, Issue 5095, 683-686
Copyright © 1993 by American Association for the Advancement of Science

articles

The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase

Y Kuroda, N Suzuki, and T Kataoka

Department of Physiology, Kobe University School of Medicine, Japan.

Ras proteins undergo a series of posttranslational modifications that are critical for their cellular function. These modifications are necessary to anchor Ras proteins to the membrane. Yeast Ras2 proteins were purified with various degrees of modification and examined for their ability to activate their effector, adenylyl cyclase. The farnesylated intermediate form of Ras2 had more than 100 times higher affinity for adenylyl cyclase than for the unprocessed form. The subsequent palmitoylation reaction had little effect. In contrast, palmitoylation was required for efficient membrane localization of the Ras2 protein. These results indicate the importance of farnesylation in the interaction of Ras2 with its effector.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Carboxyl-terminal Region of the Geranylgeranyl Diphosphate Synthase is Indispensable for the Stabilization of the Region Involved in Substrate Binding and Catalysis.
Y. Matsumura, T. Kidokoro, Y. Miyagi, N. R. Marilingaiah, and H. Sagami (2007)
J. Biochem. 142, 533-537
   Abstract »    Full Text »    PDF »
Role of the Guanine Nucleotide Exchange Factor Ost in Negative Regulation of Receptor Endocytosis by the Small GTPase Rac1.
K. Ieguchi, S. Ueda, T. Kataoka, and T. Satoh (2007)
J. Biol. Chem. 282, 23296-23305
   Abstract »    Full Text »    PDF »
Glucose Signaling in Saccharomyces cerevisiae.
G. M. Santangelo (2006)
Microbiol. Mol. Biol. Rev. 70, 253-282
   Abstract »    Full Text »    PDF »
Prenylation-Defective Human Connexin32 Mutants Are Normally Localized and Function Equivalently to Wild-Type Connexin32 in Myelinating Schwann Cells.
Y. Huang, E. E. Sirkowski, J. T. Stickney, and S. S. Scherer (2005)
J. Neurosci. 25, 7111-7120
   Abstract »    Full Text »    PDF »
Signaling Specificity by Ras Family GTPases Is Determined by the Full Spectrum of Effectors They Regulate.
P. Rodriguez-Viciana, C. Sabatier, and F. McCormick (2004)
Mol. Cell. Biol. 24, 4943-4954
   Abstract »    Full Text »    PDF »
The Pseudorabies Virus Us2 Protein, a Virion Tegument Component, Is Prenylated in Infected Cells.
A. C. Clase, M. G. Lyman, T. del Rio, J. A. Randall, C. M. Calton, L. W. Enquist, and B. W. Banfield (2003)
J. Virol. 77, 12285-12298
   Abstract »    Full Text »    PDF »
Palmitoylation and Plasma Membrane Localization of Ras2p by a Nonclassical Trafficking Pathway in Saccharomyces cerevisiae.
X. Dong, D. A. Mitchell, S. Lobo, L. Zhao, D. J. Bartels, and R. J. Deschenes (2003)
Mol. Cell. Biol. 23, 6574-6584
   Abstract »    Full Text »    PDF »
Erf4p and Erf2p Form an Endoplasmic Reticulum-associated Complex Involved in the Plasma Membrane Localization of Yeast Ras Proteins.
L. Zhao, S. Lobo, X. Dong, A. D. Ault, and R. J. Deschenes (2002)
J. Biol. Chem. 277, 49352-49359
   Abstract »    Full Text »    PDF »
Critical Function of the Ras-associating Domain as a Primary Ras-binding Site for Regulation of Saccharomyces cerevisiae Adenylyl Cyclase.
M. Kido, F. Shima, T. Satoh, T. Asato, K.-i. Kariya, and T. Kataoka (2002)
J. Biol. Chem. 277, 3117-3123
   Abstract »    Full Text »    PDF »
The Multispanning Membrane Protein Ste24p Catalyzes CAAX Proteolysis and NH2-terminal Processing of the Yeast a-Factor Precursor.
A. Tam, W. K. Schmidt, and S. Michaelis (2001)
J. Biol. Chem. 276, 46798-46806
   Abstract »    Full Text »    PDF »
Identification and Characterization of RA-GEF-2, a Rap Guanine Nucleotide Exchange Factor That Serves as a Downstream Target of M-Ras.
X. Gao, T. Satoh, Y. Liao, C. Song, C.-D. Hu, K.-i. Kariya, and T. Kataoka (2001)
J. Biol. Chem. 276, 42219-42225
   Abstract »    Full Text »    PDF »
Small GTP-Binding Proteins.
Y. Takai, T. Sasaki, and T. Matozaki (2001)
Physiol Rev 81, 153-208
   Abstract »    Full Text »    PDF »
Association of Yeast Adenylyl Cyclase with Cyclase-Associated Protein CAP Forms a Second Ras-Binding Site Which Mediates Its Ras-Dependent Activation.
F. Shima, T. Okada, M. Kido, H. Sen, Y. Tanaka, M. Tamada, C.-D. Hu, Y. Yamawaki-Kataoka, K.-i. Kariya, and T. Kataoka (2000)
Mol. Cell. Biol. 20, 26-33
   Abstract »    Full Text »
RA-GEF, a Novel Rap1A Guanine Nucleotide Exchange Factor Containing a Ras/Rap1A-associating Domain, Is Conserved between Nematode and Humans.
Y. Liao, K.-i. Kariya, C.-D. Hu, M. Shibatohge, M. Goshima, T. Okada, Y. Watari, X. Gao, T.-G. Jin, Y. Yamawaki-Kataoka, et al. (1999)
J. Biol. Chem. 274, 37815-37820
   Abstract »    Full Text »    PDF »
Nuclear DEAF-1-related (NUDR) Protein Contains a Novel DNA Binding Domain and Represses Transcription of the Heterogeneous Nuclear Ribonucleoprotein A2/B1 Promoter.
R. J. Michelson, M. W. Collard, A. J. Ziemba, J. Persinger, B. Bartholomew, and J. I. Huggenvik (1999)
J. Biol. Chem. 274, 30510-30519
   Abstract »    Full Text »    PDF »
Prenylated Prelamin A Interacts with Narf, a Novel Nuclear Protein.
R. M. Barton and H. J. Worman (1999)
J. Biol. Chem. 274, 30008-30018
   Abstract »    Full Text »    PDF »
The Strength of Interaction at the Raf Cysteine-Rich Domain Is a Critical Determinant of Response of Raf to Ras Family Small GTPases.
T. Okada, C.-D. Hu, T.-G. Jin, K.-i. Kariya, Y. Yamawaki-Kataoka, and T. Kataoka (1999)
Mol. Cell. Biol. 19, 6057-6064
   Abstract »    Full Text »    PDF »
The Prostacyclin Receptor Is Isoprenylated. ISOPRENYLATION IS REQUIRED FOR EFFICIENT RECEPTOR-EFFECTOR COUPLING.
J. S. Hayes, O. A. Lawler, M.-T. Walsh, and B. T. Kinsella (1999)
J. Biol. Chem. 274, 23707-23718
   Abstract »    Full Text »    PDF »
Human Geranylgeranyl Diphosphate Synthase. cDNA CLONING AND EXPRESSION.
T. Kuzuguchi, Y. Morita, I. Sagami, H. Sagami, and K. Ogura (1999)
J. Biol. Chem. 274, 5888-5894
   Abstract »    Full Text »    PDF »
A Non-farnesylated Ha-Ras Protein Can Be Palmitoylated and Trigger Potent Differentiation and Transformation.
M. A. Booden, T. L. Baker, P. A. Solski, C. J. Der, S. G. Punke, and J. E. Buss (1999)
J. Biol. Chem. 274, 1423-1431
   Abstract »    Full Text »    PDF »
Effect of Phosphorylation on Activities of Rap1A to Interact with Raf-1 and to Suppress Ras-dependent Raf-1 Activation.
C.-D. Hu, K.-i. Kariya, T. Okada, X. Qi, C. Song, and T. Kataoka (1999)
J. Biol. Chem. 274, 48-51
   Abstract »    Full Text »    PDF »
Characterization of a Nuclear Deformed Epidermal Autoregulatory Factor-1 (DEAF-1)-Related (NUDR) Transcriptional Regulator Protein.
J. I. Huggenvik, R. J. Michelson, M. W. Collard, A. J. Ziemba, P. Gurley, and K. A. Mowen (1998)
Mol. Endocrinol. 12, 1619-1639
   Abstract »    Full Text »
Prenylcysteine alpha -Carboxyl Methyltransferase in Suspension-Cultured Tobacco Cells.
D. N. Crowell, S. E. Sen, and S. K. Randall (1998)
Plant Physiology 118, 115-123
   Abstract »    Full Text »
Reconstitution of alpha 2D-Adrenergic Receptor Coupling to Phospholipase D in a PC12 Cell Lysate.
A. Jinsi-Parimoo and R. C. Deth (1997)
J. Biol. Chem. 272, 14556-14561
   Abstract »    Full Text »    PDF »
In Vitro Assay and Characterization of the Farnesylation-dependent Prelamin A Endoprotease.
F. Kilic, M. B. Dalton, S. K. Burrell, J. P. Mayer, S. D. Patterson, and M. Sinensky (1997)
J. Biol. Chem. 272, 5298-5304
   Abstract »    Full Text »    PDF »
The Effects of Palmitoylation on Membrane Association of Semliki Forest Virus RNA Capping Enzyme.
P. Laakkonen, T. Ahola, and L. Kaariainen (1996)
J. Biol. Chem. 271, 28567-28571
   Abstract »    Full Text »    PDF »
Palmitoylation of Ha-Ras Facilitates Membrane Binding, Activation of Downstream Effectors, and Meiotic Maturation in Xenopus Oocytes.
T. Dudler and M. H. Gelb (1996)
J. Biol. Chem. 271, 11541-11547
   Abstract »    Full Text »    PDF »
Differential Structural Requirements for Interaction of Ras Protein with Its Distinct Downstream Effectors.
K. Akasaka, M. Tamada, F. Wang, K.-i. Kariya, F. Shima, A. Kikuchi, M. Yamamoto, M. Shirouzu, S. Yokoyama, and T. Kataoka (1996)
J. Biol. Chem. 271, 5353-5360
   Abstract »    Full Text »    PDF »
Post-translational Modification of H-Ras Is Required for Activation of, but Not for Association with, B-Raf.
T. Okada, T. Masuda, M. Shinkai, K.-i. Kariya, and T. Kataoka (1996)
J. Biol. Chem. 271, 4671-4678
   Abstract »    Full Text »    PDF »
The Farnesyl Group of H-Ras Facilitates the Activation of a Soluble Upstream Activator of Mitogen-activated Protein Kinase.
P. McGeady, S. Kuroda, K. Shimizu, Y. Takai, and M. H. Gelb (1995)
J. Biol. Chem. 270, 26347-26351
   Abstract »    Full Text »    PDF »
Purification and Characterization of REKS from Xenopus Eggs.
S. Kuroda, K. Shimizu, B. Yamamori, S. Matsuda, K. Imazumi, K. Kaibuchi, and Y. Takai (1995)
J. Biol. Chem. 270, 2460-2465
   Abstract »    Full Text »    PDF »
Protein Kinase Byr2 Is a Target of Ras1 in the Fission Yeast Schizosaccharomyces pombe.
T. Masuda, K.-i. Kariya, M. Shinkai, T. Okada, and T. Kataoka (1995)
J. Biol. Chem. 270, 1979-1982
   Abstract »    Full Text »    PDF »
Protein prenylation: a mediator of protein-protein interactions.
C. Marshall (1993)
Science 259, 1865-1866
   PDF »
Analysis of the Role of the Hypervariable Region of Yeast Ras2p and Its Farnesylation in the Interaction with Exchange Factors and Adenylyl Cyclase.
J.-B. Crechet, E. Jacquet, A. Bernardi, and A. Parmeggiani (2000)
J. Biol. Chem. 275, 17754-17761
   Abstract »    Full Text »    PDF »
Mutation of Ha-Ras C Terminus Changes Effector Pathway Utilization.
M. A. Booden, D. S. Sakaguchi, and J. E. Buss (2000)
J. Biol. Chem. 275, 23559-23568
   Abstract »    Full Text »    PDF »
Membrane Localization of Raf Assists Engagement of Downstream Effectors.
M. A. Farrar, J. Tian, and R. M. Perlmutter (2000)
J. Biol. Chem. 275, 31318-31324
   Abstract »    Full Text »    PDF »
Regulation of a Novel Human Phospholipase C, PLCepsilon , through Membrane Targeting by Ras.
C. Song, C.-D. Hu, M. Masago, K.-i. Kariya, Y. Yamawaki-Kataoka, M. Shibatohge, D. Wu, T. Satoh, and T. Kataoka (2001)
J. Biol. Chem. 276, 2752-2757
   Abstract »    Full Text »    PDF »
Role of the CDC25 Homology Domain of Phospholipase Cepsilon in Amplification of Rap1-dependent Signaling.
T.-G. Jin, T. Satoh, Y. Liao, C. Song, X. Gao, K.-i. Kariya, C.-D. Hu, and T. Kataoka (2001)
J. Biol. Chem. 276, 30301-30307
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)