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Protein Post-translational Modification in Human Diseases
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Protein Post-translational Modification in Human Diseases

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 12755

Special Issue Editors

Dr. Aida Serra

E-Mail Website
Guest Editor
1. IMDEA Food & Health Sciences Research Institute, +Pec Proteomics, Campus of International Excellence UAM+CSIC, Old Cantoblanco Hospital, 8 Crta. Canto Blanco, 28049 Madrid, Spain
2. Proteored-Instituto de Salud Carlos III (ISCIII), Madrid, Spain
Interests: proteomics; neurodegeneration; extracellular vesicles; protein post-translational modifications; degenerative protein modifications; metabolism; human diseases
Special Issues, Collections and Topics in MDPI journals
Dr. Xavier Gallart-Palau

E-Mail Website
Co-Guest Editor
1. Institut d'Investigació Sanitària Pere Virgili (IISPV), Reus, Spain
2. Carlos III Health Institute (Instituto de Salud Carlos III), Madrid, Spain
Interests: neurochemistry; proteinopathy; Alzheimer’s disease; vascular dementia; neurovascular unit; extracellular vesicles; proteomics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Proteins’ post-translational modifications (PTMs) are covalently attached protein decorations of enzymatic or spontaneous origin, known to modulate and expand the functionality of proteomes. Similarly, these protein decorations have demonstrated an ability to influence and regulate several biological processes at systemic levels. The presence/absence of certain PTMs can interfere with the normal functions of proteins, for example, increasing protein malfunction and aggregability. Therefore, aberrant PTM profiles have been associated with multiple diseases and pathological conditions. The mechanisms behind the molecular outcomes of aberrant PTM profiles in biological proteomes require specific investigation and remain a current, paramount field in biomedicine.

Thus, this Special Issue focuses on the generation of knowledge based on the scientific investigation of the role(s) of PTMs in human health and disease conditions by systems biology and other scientific methodologies.

Dr. Aida Serra
Guest Editor, Topic Editor
Dr. Xavier Gallart-Palau
Co-Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

proteins
post-translational modifications
PTMs
protein decorations
proteomes

Published Papers (4 papers)

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Review

18 pages, 1712 KiB  
Review
Implications of Post-Translational Modifications in Autoimmunity with Emphasis on Citrullination, Homocitrullination and Acetylation for the Pathogenesis, Diagnosis and Prognosis of Rheumatoid Arthritis
by Isabel Haro, Raimon Sanmartí and María J. Gómara
Int. J. Mol. Sci. 2022, 23(24), 15803; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms232415803 - 13 Dec 2022
Cited by 7 | Viewed by 2106
Abstract
Post-translational modifications (PTMs) influence cellular processes and consequently, their dysregulation is related to the etiologies of numerous diseases. It is widely known that a variety of autoimmune responses in human diseases depend on PTMs of self-proteins. In this review we summarize the latest [...] Read more.
Post-translational modifications (PTMs) influence cellular processes and consequently, their dysregulation is related to the etiologies of numerous diseases. It is widely known that a variety of autoimmune responses in human diseases depend on PTMs of self-proteins. In this review we summarize the latest findings about the role of PTMs in the generation of autoimmunity and, specifically, we address the most relevant PTMs in rheumatic diseases that occur in synovial tissue. Citrullination, homocitrullination (carbamylation) and acetylation are responsible for the generation of Anti-Modified Protein/Peptide Antibodies (AMPAs family), autoantibodies which have been implicated in the etiopathogenesis, diagnosis and prognosis of rheumatoid arthritis (RA). Synthetic peptides provide complete control over the exact epitopes presented as well as the specific positions in their sequence where post-translationally modified amino acids are located and are key to advancing the detection of serological RA biomarkers that could be useful to stratify RA patients in order to pursue a personalized rheumatology. In this review we specifically address the latest findings regarding synthetic peptides post-translationally modified for the specific detection of autoantibodies in RA patients. Full article
(This article belongs to the Special Issue Protein Post-translational Modification in Human Diseases)
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29 pages, 11990 KiB  
Review
Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization
by Aleksandra Marchwicka, Daria Kamińska, Mohsen Monirialamdari, Katarzyna M. Błażewska and Edyta Gendaszewska-Darmach
Int. J. Mol. Sci. 2022, 23(10), 5424; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23105424 - 12 May 2022
Cited by 14 | Viewed by 3158
Abstract
Protein prenylation is a post-translational modification controlling the localization, activity, and protein–protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase [...] Read more.
Protein prenylation is a post-translational modification controlling the localization, activity, and protein–protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase-I), Rab geranylgeranyltransferase (GGTase-II), and recently discovered geranylgeranyltransferase type III (GGTase-III). Blocking small GTPase activity, namely inhibiting prenyltransferases, has been proposed as a potential disease treatment method. Inhibitors of prenyltransferase have resulted in substantial therapeutic benefits in various diseases, such as cancer, neurological disorders, and viral and parasitic infections. In this review, we overview the structure of FTase, GGTase-I, GGTase-II, and GGTase-III and summarize the current status of research on their inhibitors. Full article
(This article belongs to the Special Issue Protein Post-translational Modification in Human Diseases)
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14 pages, 2439 KiB  
Review
Past and Future Strategies to Inhibit Membrane Localization of the KRAS Oncogene
by Malak Haidar and Patrick Jacquemin
Int. J. Mol. Sci. 2021, 22(24), 13193; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222413193 - 07 Dec 2021
Cited by 8 | Viewed by 2680
Abstract
KRAS is one of the most studied oncogenes. It is well known that KRAS undergoes post-translational modifications at its C-terminal end. These modifications are essential for its membrane location and activity. Despite significant efforts made in the past three decades to target the [...] Read more.
KRAS is one of the most studied oncogenes. It is well known that KRAS undergoes post-translational modifications at its C-terminal end. These modifications are essential for its membrane location and activity. Despite significant efforts made in the past three decades to target the mechanisms involved in its membrane localization, no therapies have been approved and taken into the clinic. However, many studies have recently reintroduced interest in the development of KRAS inhibitors, either by directly targeting KRAS or indirectly through the inhibition of critical steps involved in post-translational KRAS modifications. In this review, we summarize the approaches that have been applied over the years to inhibit the membrane localization of KRAS in cancer and propose a new anti-KRAS strategy that could be used in clinic. Full article
(This article belongs to the Special Issue Protein Post-translational Modification in Human Diseases)
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25 pages, 1687 KiB  
Review
ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control
by Palmiro Poltronieri, Masanao Miwa and Mitsuko Masutani
Int. J. Mol. Sci. 2021, 22(19), 10829; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms221910829 - 07 Oct 2021
Cited by 10 | Viewed by 4083
Abstract
Among the post-translational modifications of proteins, ADP-ribosylation has been studied for over fifty years, and a large set of functions, including DNA repair, transcription, and cell signaling, have been assigned to this post-translational modification (PTM). This review presents an update on the function [...] Read more.
Among the post-translational modifications of proteins, ADP-ribosylation has been studied for over fifty years, and a large set of functions, including DNA repair, transcription, and cell signaling, have been assigned to this post-translational modification (PTM). This review presents an update on the function of a large set of enzyme writers, the readers that are recruited by the modified targets, and the erasers that reverse the modification to the original amino acid residue, removing the covalent bonds formed. In particular, the review provides details on the involvement of the enzymes performing monoADP-ribosylation/polyADP-ribosylation (MAR/PAR) cycling in cancers. Of note, there is potential for the application of the inhibitors developed for cancer also in the therapy of non-oncological diseases such as the protection against oxidative stress, the suppression of inflammatory responses, and the treatment of neurodegenerative diseases. This field of studies is not concluded, since novel enzymes are being discovered at a rapid pace. Full article
(This article belongs to the Special Issue Protein Post-translational Modification in Human Diseases)
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