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Considering Protonation as a Posttranslational Modification Regulating Protein Structure and Function
Open accessAbstract
Posttranslational modification is an evolutionarily conserved mechanism for regulating protein activity, binding affinity, and stability. Compared with established posttranslational modifications such as phosphorylation or ubiquitination, posttranslational modification by protons within physiological pH ranges is a less recognized mechanism for regulating protein function. By changing the charge of amino acid side chains, posttranslational modification by protons can drive dynamic changes in protein conformation and function. Addition and removal of a proton is rapid and reversible and, in contrast to most other posttranslational modifications, does not require an enzyme. Signaling specificity is achieved by only a minority of sites in proteins titrating within the physiological pH range. Here, we examine the structural mechanisms and functional consequences of proton posttranslational modification of pH-sensing proteins regulating different cellular processes.
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Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
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ADF/Cofilin: a functional node in cell biology
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EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells
van Rheenen, J., Song, X., van Roosmalen, W., Cammer, M., Chen, X., DesMarais, V., Yip, S.-C., Backer, J. M., Eddy, R. J., & Condeelis, J. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706206 · Cited by 244
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pH sensing and regulation in cancer
Damaghi, M., Wojtkowiak, J. W., & Gillies, R. J. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00370 · Cited by 536
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Evidence-based Guidelines for Controlling pH in Mammalian Live-Cell Culture Systems
Michl, J., Park, K. C., & Swietach, P. (2019) · Communications Biology · doi:10.1038/s42003-019-0393-7 · Cited by 267
Talin as a mechanosensitive signaling hub
Goult, B. T., Yan, J., & Schwartz, M. A. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201808061 · Cited by 250
Physiological Roles of Acid-Base Sensors
Levin, L. R., & Buck, J. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071821 · Cited by 109
Metadata
- Authors
- Schönichen, A., Webb, B. A., Jacobson, M. P., & Barber, D. L.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2013-05-06
- Volume
- 42
- Issue
- 1
- Pages
- 289-314
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2148814198
- Cited by
- 162
- References
- 8
- FWCI
- 0.77
- Type
- journal article
- Language
- en
- Open access
- green
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