The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
The next level of complexity: Crosstalk of posttranslational modifications
Abstract
Beside gene expression and translational control, which are relatively slow, PTM of proteins represents the major level of regulation, from very fast and reversible to slow or irreversible processes. PTM s affect protein structure and act as molecular switches, which regulate the interaction of proteins with DNA , cofactors, lipids, and other proteins. In the past few years, evidence for extensive crosstalk between PTM s has accumulated. The combination of different PTM s on protein surfaces can create a “ PTM code,” which can be recognized by specific effectors to initiate/inhibit downstream events, only inducing/retaining a signal once the complementary incoming signals are present at the same time and place. Although MS ‐based proteomics has substantially improved our knowledge about PTM s, currently sensitive and dedicated analytical strategies are available only for few different types of PTM . Several recent studies focused on the combinatorial analysis of PTM s, but preferentially utilized peptide‐centric bottom‐up strategies might be too restricted to decipher complex PTM codes. Here, we discuss the current state of PTM crosstalk research and how proteomics may contribute to understanding PTM codes, representing the next level of complexity and one of the biggest challenges for future proteomics research.
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Cites
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Cited by
Regulating tumor suppressor genes: post-translational modifications
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Phosphoproteomics in the Age of Rapid and Deep Proteome Profiling
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Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications
Doll, S., & Burlingame, A. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500904b · Cited by 261
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Metadata
- Authors
- Venne, A. S., Kollipara, L., & Zahedi, R. P.
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2014-01-06
- Volume
- 14
- Issue
- 4-5
- Pages
- 513-524
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- OpenAlex
- W2022922908
- Cited by
- 323
- References
- 14
- FWCI
- 6.14
- Type
- journal article
- Language
- en
- Open access
- closed
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- Venne, A. S., Kollipara, L., & Zahedi, R. P. (2014). The next level of complexity: Crosstalk of posttranslational modifications. PROTEOMICS. https://doi.org/10.1002/pmic.201300344
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