Research Topic

Post-Translational Modifications - The Dark Matter of Biology in Health and Disease

About this Research Topic

Humans have just 20,000 genes controlling the complex phenotype we observe. The diversity in proteins may better explain the complexity based on isoforms and modifications that increase the number by several orders of magnitude. Protein post translational modifications (PTM) form the dark matter of biology- the hidden regulatory layer controlling protein folding, stability, activity, protein localization, interactions and turnover. These processes drive cellular homeostasis and any perturbation may lead to a disease. Although PTMs may help in network rewiring to avert subtle undesired changes, their complex interplay and crosstalk determines cell fate. More than 300 biological PTMs are known but only few subjected to in-depth analysis due to various challenges involved. However, as researchers are recognizing their importance, the list of modification sites and the methods to study them on large scale keep improving. The role of PTMs in diseases is beginning to be appreciated with increasing depth and coverage. New sites of important PTMs like phosphorylation, acetylation, glycosylation, ubiquitination, SUMOylation etc are continually being discovered. Less studied modifications like crotonylation, malonylation, MARylation etc are also being investigated with increased vigor. Focus is shifting to PTMs in mainstream biology and functional importance is being assessed for the sites discovered and their roles in driving biological decisions in protein-protein interactions and networks besides cellular localization and enzymatic activity.

This Research Topic focuses on, but is not limited to:

(i) Systems level analysis of PTMs and their cross-talks.
(ii) Tools and innovative methods for sample preparation and enrichment strategies to study specific PTMs.
(iii) Application of mass spectrometry techniques to study PTMs at their sub-stoichiometric concentrations using data-independent acquisition methods (DIA) or targeted methods.
(iv) Improvement in data analysis algorithms, site localization and better spectral matching for modified peptides.
(v) Integrated network or protein interaction analysis to decipher in-depth biology
(vi) Statistical algorithms to remove spurious hits, data visualization of large scale PTM
(vii) Discerning biological roles of PTMs in diseases


Keywords: Post-translational modifications, disease, localization, interactions, signaling, networks


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

Humans have just 20,000 genes controlling the complex phenotype we observe. The diversity in proteins may better explain the complexity based on isoforms and modifications that increase the number by several orders of magnitude. Protein post translational modifications (PTM) form the dark matter of biology- the hidden regulatory layer controlling protein folding, stability, activity, protein localization, interactions and turnover. These processes drive cellular homeostasis and any perturbation may lead to a disease. Although PTMs may help in network rewiring to avert subtle undesired changes, their complex interplay and crosstalk determines cell fate. More than 300 biological PTMs are known but only few subjected to in-depth analysis due to various challenges involved. However, as researchers are recognizing their importance, the list of modification sites and the methods to study them on large scale keep improving. The role of PTMs in diseases is beginning to be appreciated with increasing depth and coverage. New sites of important PTMs like phosphorylation, acetylation, glycosylation, ubiquitination, SUMOylation etc are continually being discovered. Less studied modifications like crotonylation, malonylation, MARylation etc are also being investigated with increased vigor. Focus is shifting to PTMs in mainstream biology and functional importance is being assessed for the sites discovered and their roles in driving biological decisions in protein-protein interactions and networks besides cellular localization and enzymatic activity.

This Research Topic focuses on, but is not limited to:

(i) Systems level analysis of PTMs and their cross-talks.
(ii) Tools and innovative methods for sample preparation and enrichment strategies to study specific PTMs.
(iii) Application of mass spectrometry techniques to study PTMs at their sub-stoichiometric concentrations using data-independent acquisition methods (DIA) or targeted methods.
(iv) Improvement in data analysis algorithms, site localization and better spectral matching for modified peptides.
(v) Integrated network or protein interaction analysis to decipher in-depth biology
(vi) Statistical algorithms to remove spurious hits, data visualization of large scale PTM
(vii) Discerning biological roles of PTMs in diseases


Keywords: Post-translational modifications, disease, localization, interactions, signaling, networks


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

31 December 2017 Abstract
31 March 2018 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

31 December 2017 Abstract
31 March 2018 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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