The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Autoinhibitory Domains: Modular Effectors of Cellular Regulation
Abstract
▪ Abstract Autoinhibitory domains are regions of proteins that negatively regulate the function of other domains via intramolecular interactions. Autoinhibition is a potent regulatory mechanism that provides tight “on-site” repression. The discovery of autoinhibition generates valuable clues to how a protein is regulated within a biological context. Mechanisms that counteract the autoinhibition, including proteolysis, post-translational modifications, as well as addition of proteins or small molecules in trans, often represent central regulatory pathways. In this review, we document the diversity of instances in which autoinhibition acts in cell regulation. Seven well-characterized examples (e.g., σ 70, Ets-1, ERM, SNARE and WASP proteins, SREBP, Src) are covered in detail. Over thirty additional examples are listed. We present experimental approaches to characterize autoinhibitory domains and discuss the implications of this widespread phenomenon for biological regulation in both the normal and diseased states.
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Cites
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871
DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
STEHELIN, D., VARMUS, H. E., BISHOP, J. M., & VOGT, P. K. (1976) · Nature · doi:10.1038/260170a0 · Cited by 1,321 · cited 1×
“IDENTIFICATION OF INHIBITORY ELEMENTS Autoinhibition of Src kinase was discovered in the context of an oncogenic version of Src. v-Src kinase, encoded by Rous sarcoma virus, is responsible for cell transformation by this retrovirus (Stehelin et al. 1976).”
BackgroundThe ETS-domain transcription factor family
Sharrocks, A. D. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35099076 · Cited by 1,086 · cited 1×
“The founding member of theetsgene family, Ets-1, illustrates the many layers of regulation that generate specificity for its DNA-binding activity (Graves & Petersen 1998, Sharrocks 2001).”
BackgroundScar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E., & Pollard, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3739 · Cited by 773
Specificity within the ets Family of Transcription Factors
(1998) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60738-1 · Cited by 344
Self-citationA new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex
Kodandapani, R., Pio, F., Ni, C.-Z., Piccialli, G., Klemsz, M., McKercher, S., Maki, R. A., & Ely, K. R. (1996) · Nature · doi:10.1038/380456a0 · Cited by 315 · cited 1×
“High-resolution molecular models of the ETS domain in contact with DNA provided further insight (Batchelor et al. 1998; Garvie et al. 2001; Kodandapani et al. 1996; Mo et al. 1998, 2000).”
BackgroundStructure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions
Volkmann, N., Amann, K. J., Stoilova-McPhie, S., Egile, C., Winter, D. C., Hazelwood, L., Heuser, J. E., Li, R., Pollard, T. D., & Hanein, D. (2001) · Science · doi:10.1126/science.1063025 · Cited by 258
Brass, A. L., Kehrli, E., Eisenbeis, C. F., Storb, U., & Singh, H. (1996) · Genes & Development · doi:10.1101/gad.10.18.2335 · Cited by 242
Kim, W., Sieweke, M., Ogawa, E., Wee, H., Englmeier, U., Graf, T., & Ito, Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1609 · Cited by 230
Cited by
Targeting transcription factors in cancer — from undruggable to reality
Bushweller, J. H. (2019) · Nature Reviews Cancer · doi:10.1038/s41568-019-0196-7 · Cited by 919
Genomic and biochemical insights into the specificity of ETS transcription factors
Hollenhorst, P. C., McIntosh, L. P., & Graves, B. J. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.79.081507.103945 · Cited by 490
Self-citationHeme is involved in microRNA processing
Faller, M., Matsunaga, M., Yin, S., Loo, J. A., & Guo, F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1182 · Cited by 295
Reprogramming Control of an Allosteric Signaling Switch Through Modular Recombination
Dueber, J. E., Yeh, B. J., Chak, K., & Lim, W. A. (2003) · Science · doi:10.1126/science.1085945 · Cited by 296
Reciprocal Activation within a Kinase-Effector Complex Underlying Persistence of Structural LTP
Saneyoshi, T., Matsuno, H., Suzuki, A., Murakoshi, H., Hedrick, N. G., Agnello, E., O’Connell, R., Stratton, M. M., Yasuda, R., & Hayashi, Y. (2019) · Neuron · doi:10.1016/j.neuron.2019.04.012 · Cited by 119
Metadata
- Authors
- Pufall, M. A., & Graves, B. J.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2002-11
- Volume
- 18
- Issue
- 1
- Pages
- 421-462
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2096170764
- Cited by
- 236
- References
- 19
- FWCI
- 0.52
- Type
- journal article
- Language
- en
- Open access
- closed
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