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Protein-Protein Interactions in Cellular Function

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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 (28 November 2023) | Viewed by 4909

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Special Issue Editor

Prof. Dr. Kevin H. Mayo

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Guest Editor

Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN 55455, USA
Interests: structural biology; NMR spectroscopy; biophysical methods; protein and carbohydrate structures and their interactions; galectins; chemokines; drug development and discovery; angiogenesis; oncology; cardiovascular disease

Special Issue Information

Dear Colleagues,

Numerous protein-protein interactions occur in cells to effectively dictate function. Often these complexes associate and dissociate with K_D’s in the micromolar range depending on their physiological concentration and their overall intra- and inter-cellular environment. Here, we focus on small molecule effector proteins galectins and chemokines, their structural interactions as homo- and hetero-oligomers, ligand binding effects, and interactions with their cell receptors. Inter-molecular interactions are discussed in the context of the biophysical techniques (e.g. X-ray, NMR, Cryo-EM, MD simulations) used to elucidate structural information, as well as the impact of their interactions on physiological function.

Prof. Dr. Kevin H. Mayo
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
carbohydrates
cell receptors
galectins
chemokines
molecular interactions
structural biology
biophysical techniques
oncology
cardiovascular disease

Published Papers (4 papers)

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Research

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24 pages, 13257 KiB

Open AccessArticle

Molecular Relay Stations in Membrane Nanotubes: IRSp53 Involved in Actin-Based Force Generation

by Tamás Madarász, Brigitta Brunner, Henriett Halász, Elek Telek, János Matkó, Miklós Nyitrai and Edina Szabó-Meleg

Int. J. Mol. Sci. 2023, 24(17), 13112; https://doi.org/10.3390/ijms241713112 - 23 Aug 2023

Cited by 1 | Viewed by 1061

Abstract

Membrane nanotubes are cell protrusions that grow to tens of micrometres and functionally connect cells. Actin filaments are semi-flexible polymers, and their polymerisation provides force for the formation and growth of membrane nanotubes. The molecular bases for the provision of appropriate force through such long distances are not yet clear. Actin filament bundles are likely involved in these processes; however, even actin bundles weaken when growing over long distances, and there must be a mechanism for their regeneration along the nanotubes. We investigated the possibility of the formation of periodic molecular relay stations along membrane nanotubes by describing the interactions of actin with full-length IRSp53 protein and its N-terminal I-BAR domain. We concluded that I-BAR is involved in the early phase of the formation of cell projections, while IRSp53 is also important for the elongation of protrusions. Considering that IRSp53 binds to the membrane along the nanotubes and nucleates actin polymerisation, we propose that, in membrane nanotubes, IRSp53 establishes molecular relay stations for actin polymerisation and, as a result, supports the generation of force required for the growth of nanotubes. Full article

(This article belongs to the Special Issue Protein-Protein Interactions in Cellular Function)

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Review

Jump to: Research

21 pages, 1992 KiB

Open AccessReview

Heterologous Interactions with Galectins and Chemokines and Their Functional Consequences

by Kevin H. Mayo

Int. J. Mol. Sci. 2023, 24(18), 14083; https://doi.org/10.3390/ijms241814083 - 14 Sep 2023

Cited by 1 | Viewed by 813

Abstract

Extra- and intra-cellular activity occurs under the direction of numerous inter-molecular interactions, and in any tissue or cell, molecules are densely packed, thus promoting those molecular interactions. Galectins and chemokines, the focus of this review, are small, protein effector molecules that mediate various cellular functions—in particular, cell adhesion and migration—as well as cell signaling/activation. In the past, researchers have reported that combinations of these (and other) effector molecules act separately, yet sometimes in concert, but nevertheless physically apart and via their individual cell receptors. This view that each effector molecule functions independently of the other limits our thinking about functional versatility and cooperation, and, in turn, ignores the prospect of physiologically important inter-molecular interactions, especially when both molecules are present or co-expressed in the same cellular environment. This review is focused on such protein-protein interactions with chemokines and galectins, the homo- and hetero-oligomeric structures that they can form, and the functional consequences of those paired interactions. Full article

(This article belongs to the Special Issue Protein-Protein Interactions in Cellular Function)

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23 pages, 1500 KiB

Open AccessReview

Heterodimers Are an Integral Component of Chemokine Signaling Repertoire

by Kimia Kaffashi, Didier Dréau and Irina V. Nesmelova

Int. J. Mol. Sci. 2023, 24(14), 11639; https://doi.org/10.3390/ijms241411639 - 19 Jul 2023

Viewed by 1252

Abstract

Chemokines are a family of signaling proteins that play a crucial role in cell–cell communication, cell migration, and cell trafficking, particularly leukocytes, under both normal and pathological conditions. The oligomerization state of chemokines influences their biological activity. The heterooligomerization occurs when multiple chemokines spatially and temporally co-localize, and it can significantly affect cellular responses. Recently, obligate heterodimers have emerged as tools to investigate the activities and molecular mechanisms of chemokine heterodimers, providing valuable insights into their functional roles. This review focuses on the latest progress in understanding the roles of chemokine heterodimers and their contribution to the functioning of the chemokine network. Full article

(This article belongs to the Special Issue Protein-Protein Interactions in Cellular Function)

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18 pages, 876 KiB

Open AccessReview

Chemokine Heteromers and Their Impact on Cellular Function—A Conceptual Framework

by Xavier Blanchet, Christian Weber and Philipp von Hundelshausen

Int. J. Mol. Sci. 2023, 24(13), 10925; https://doi.org/10.3390/ijms241310925 - 30 Jun 2023

Cited by 1 | Viewed by 1232

Abstract

Chemoattractant cytokines or chemokines are proteins involved in numerous biological activities. Their essential role consists of the formation of gradient and (immune) cell recruitment. Chemokine biology and its related signaling system is more complex than simple ligand–receptor interactions. Beside interactions with their cognate and/or atypical chemokine receptors, and glycosaminoglycans (GAGs), chemokines form complexes with themselves as homo-oligomers, heteromers and also with other soluble effector proteins, including the atypical chemokine MIF, carbohydrate-binding proteins (galectins), damage-associated molecular patterns (DAMPs) or with chemokine-binding proteins such as evasins. Likewise, nucleic acids have been described as binding targets for the tetrameric form of CXCL4. The dynamic balance between monomeric and dimeric structures, as well as interactions with GAGs, modulate the concentrations of free chemokines available along with the nature of the gradient. Dimerization of chemokines changes the canonical monomeric fold into two main dimeric structures, namely CC- and CXC-type dimers. Recent studies highlighted that chemokine dimer formation is a frequent event that could occur under pathophysiological conditions. The structural changes dictated by chemokine dimerization confer additional biological activities, e.g., biased signaling. The present review will provide a short overview of the known functionality of chemokines together with the consequences of the interactions engaged by the chemokines with other proteins. Finally, we will present potential therapeutic tools targeting the chemokine multimeric structures that could modulate their biological functions. Full article

(This article belongs to the Special Issue Protein-Protein Interactions in Cellular Function)

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