Ubiquitin is a highly versatile post-translational modification that controls virtually all types of cellular events. Over the past ten years we have learned that diverse forms of ubiquitin modifications and of ubiquitin binding modules co-exist in the cell, giving rise to complex networks of protein:protein interactions. A central problem that continues to puzzle ubiquitinologists is how cells translate this myriad of stimuli into highly specific responses. This is a classical signalling problem. Here, we draw parallels with the phosphorylation signalling pathway and we discuss the expanding repertoire of ubiquitin signals, signal tranducers and signalling-regulated E3 enzymes. We examine recent advances in the field, including a new mechanism of regulation of E3 ligases that relies on ubiquitination. © 2007 Woelk et al; licensee BioMed Central Ltd.
CITATION STYLE
Woelk, T., Sigismund, S., Penengo, L., & Polo, S. (2007, March 13). The ubiquitination code: A signalling problem. Cell Division. https://doi.org/10.1186/1747-1028-2-11
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