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A New Finger on the Protein Destruction Button
Abstract
The timely eradication of proteins that drive cell division is vital to keeping normal growth from turning into runaway malignancy. Before proteins are eliminated, however, they have to be tagged for disposal by attachment of a small protein called ubiquitin. New research, including that reported on page 309, has identified a molecular motif--the so-called RING finger--as instrumental in bringing about that ubiquitin addition. The RING finger is present in more than 200 proteins, many of whose functions are currently unknown. So the discovery is expected to touch off a wave of research on how these proteins might regulate cell activities, and also exploration of how the chain of protein destruction might be restored in some case to halt the growth of cancer cells.
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“Current knowledge of the RING-finger domain indicates that it may have intrinsic Ub-ligase activity”
From Limb-Girdle Muscular Dystrophy Type 2H Associated with Mutation in TRIM32, a Putative E3-Ubiquitin–Ligase Gene (2002) · cites this paper as Barinaga 1999
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Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT Domain E3 Ligase
Verdecia, M. A., Joazeiro, C. A. P., Wells, N. J., Ferrer, J.-L., Bowman, M. E., Hunter, T. R., & Noel, J. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00774-8 · Cited by 288
Frosk, P., Weiler, T., Nylen, E., Sudha, T., Greenberg, C. R., Morgan, K., Fujiwara, T. M., & Wrogemann, K. (2002) · The American Journal of Human Genetics · doi:10.1086/339083 · Cited by 261
“Current knowledge of the RING-finger domain indicates that it may have intrinsic Ub-ligase activity (Barinaga 1999), and it has been suggested that all RING- finger proteins are E3-Ub ligases (Freemont 2000).”
BackgroundEvidence for Direct Interaction between Sprouty and Cbl
Wong, E. S. M., Lim, J., Low, B. C., Chen, Q., & Guy, G. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006945200 · Cited by 131
SHP2 and cbl participate in α-chemokine receptor CXCR4–mediated signaling pathways
Chernock, R. D., Cherla, R. P., & Ganju, R. K. (2001) · Blood · doi:10.1182/blood.v97.3.608 · Cited by 90
Angiotensin II early regulated genes in H295R human adrenocortical cells
Romero, D. G., Plonczynski, M. W., Vergara, G. R., Gómez-Sánchez, E. P., & Gómez-Sánchez, C. E. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00097.2004 · Cited by 59
“E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; various RING fingers exhibit binding to E2 ubiquitinconjugating enzymes (4, 33, 47).”
Background
Metadata
- Authors
- Barinaga, M.
- Corresponding author
- Barinaga, Marcia
- Venue
- Science
- Published
- 1999-10-08
- Volume
- 286
- Issue
- 5438
- Pages
- 223-225
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1637251290
- Cited by
- 8
- References
- 0
- Type
- other
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- ring finger, ubiquitin, protein degradation, ubiquitination, E3 ubiquitin ligase, cell cycle regulation, cancer, tumor suppression
- MeSH terms
- Amino Acid Sequence, Animals, Ligases, Mutation, Proteins, Proto-Oncogene Proteins, Ubiquitins, Receptors, Platelet-Derived Growth Factor, src Homology Domains, Phosphotyrosine, BRCA1 Protein, Receptor Protein-Tyrosine Kinases, Ubiquitin-Protein Ligases, Proto-Oncogene Proteins c-cbl, Mice, ErbB Receptors
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- The paper
- Barinaga, M. (1999). A New Finger on the Protein Destruction Button. Science. https://doi.org/10.1126/science.286.5438.223
