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Special Issue "Signal Transduction: From Molecular Pathways to Translational Research"

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

Deadline for manuscript submissions: 31 March 2021.

Special Issue Editors

Dr. Katharina Kubatzky
Website
Guest Editor
Department of Medical Microbiology and Hygiene, Heidelberg University Hospital, Germany
Interests: signal transduction; bone; osteoclast; bacterial infection; protein toxin
Special Issues and Collections in MDPI journals
Dr. Elisabeth Seebach
Website
Guest Editor
Department of Medical Microbiology and Hygiene, Heidelberg University Hospital, Germany
Interests: Staphylococci; bone infections; biofilm

Special Issue Information

Dear Colleagues,

Much progress has been made in the signaling field over the last twenty years; new molecules and mechanisms have been discovered and novel methods and technologies invented. While only a few specialists worked in the field in the 1990s, today, signaling pathways play a prominent role in the research of most life scientists. Nonetheless, signal transduction remains a very dynamic field that covers many aspects from basic to translational research. Our understanding of the molecular signaling pathways has made it possible to specifically design drugs that intervene at dysregulated signaling nodes or to repair missing signaling molecules through gene therapy.

This second Special Issue invites both original research articles as well as reviews, commentaries, and perspectives that cover all aspects of signal transduction. As the focus theme of this 24th meeting of the Signal Transduction Society (STS) is “target identification and intervention”, we especially welcome manuscripts that address this topic.

Addendum: The Signal Transduction Society (STS) was established in 1998 and is a non-profit organization that provides an interdisciplinary forum for scientists with an interest in signal transduction processes in cells and organisms. The STS annually organizes the “Joint Meeting Signal Transduction—Receptor, Mediators and Genes”. This year, the meeting will take place in Weimar from 2 to 3 November in a shortened form due to the COVID-19 pandemic.

https://www.sigtrans.de/meeting.html

Dr. Katharina Kubatzky
Dr. Elisabeth Seebach
Guest Editors

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 papers will be 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

  • signal transduction
  • receptor signaling
  • infection and inflammation
  • protein interaction
  • tumor biology
  • growth factors
  • cytokines
  • cell death and differentiation

Published Papers (2 papers)

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Research

Open AccessArticle
The Novel ALG-2 Target Protein CDIP1 Promotes Cell Death by Interacting with ESCRT-I and VAPA/B
Int. J. Mol. Sci. 2021, 22(3), 1175; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22031175 - 25 Jan 2021
Abstract
Apoptosis-linked gene 2 (ALG-2, also known as PDCD6) is a member of the penta-EF-hand (PEF) family of Ca2+-binding proteins. The murine gene encoding ALG-2 was originally reported to be an essential gene for apoptosis. However, the role of ALG-2 in cell [...] Read more.
Apoptosis-linked gene 2 (ALG-2, also known as PDCD6) is a member of the penta-EF-hand (PEF) family of Ca2+-binding proteins. The murine gene encoding ALG-2 was originally reported to be an essential gene for apoptosis. However, the role of ALG-2 in cell death pathways has remained elusive. In the present study, we found that cell death-inducing p53 target protein 1 (CDIP1), a pro-apoptotic protein, interacts with ALG-2 in a Ca2+-dependent manner. Co-immunoprecipitation analysis of GFP-fused CDIP1 (GFP-CDIP1) revealed that GFP-CDIP1 associates with tumor susceptibility gene 101 (TSG101), a known target of ALG-2 and a subunit of endosomal sorting complex required for transport-I (ESCRT-I). ESCRT-I is a heterotetrameric complex composed of TSG101, VPS28, VPS37 and MVB12/UBAP1. Of diverse ESCRT-I species originating from four VPS37 isoforms (A, B, C, and D), CDIP1 preferentially associates with ESCRT-I containing VPS37B or VPS37C in part through the adaptor function of ALG-2. Overexpression of GFP-CDIP1 in HEK293 cells caused caspase-3/7-mediated cell death. In addition, the cell death was enhanced by co-expression of ALG-2 and ESCRT-I, indicating that ALG-2 likely promotes CDIP1-induced cell death by promoting the association between CDIP1 and ESCRT-I. We also found that CDIP1 binds to vesicle-associated membrane protein-associated protein (VAP)A and VAPB through the two phenylalanines in an acidic tract (FFAT)-like motif in the C-terminal region of CDIP1, mutations of which resulted in reduction of CDIP1-induced cell death. Therefore, our findings suggest that different expression levels of ALG-2, ESCRT-I subunits, VAPA and VAPB may have an impact on sensitivity of anticancer drugs associated with CDIP1 expression. Full article
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Open AccessArticle
YB-1 Interferes with TNFα–TNFR Binding and Modulates Progranulin-Mediated Inhibition of TNFα Signaling
Int. J. Mol. Sci. 2020, 21(19), 7076; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21197076 - 25 Sep 2020
Abstract
Inflammation and an influx of macrophages are common elements in many diseases. Among pro-inflammatory cytokines, tumor necrosis factor α (TNFα) plays a central role by amplifying the cytokine network. Progranulin (PGRN) is a growth factor that binds to TNF receptors and interferes with [...] Read more.
Inflammation and an influx of macrophages are common elements in many diseases. Among pro-inflammatory cytokines, tumor necrosis factor α (TNFα) plays a central role by amplifying the cytokine network. Progranulin (PGRN) is a growth factor that binds to TNF receptors and interferes with TNFα-mediated signaling. Extracellular PGRN is processed into granulins by proteases released from immune cells. PGRN exerts anti-inflammatory effects, whereas granulins are pro-inflammatory. The factors coordinating these ambivalent functions remain unclear. In our study, we identify Y-box binding protein-1 (YB-1) as a candidate for this immune-modulating activity. Using a yeast-2-hybrid assay with YB-1 protein as bait, clones encoding for progranulin were selected using stringent criteria for strong interaction. We demonstrate that at physiological concentrations, YB-1 interferes with the binding of TNFα to its receptors in a dose-dependent manner using a flow cytometry-based binding assay. We show that YB-1 in combination with progranulin interferes with TNFα-mediated signaling, supporting the functionality with an NF-κB luciferase reporter assay. Together, we show that YB-1 displays immunomodulating functions by affecting the binding of TNFα to its receptors and influencing TNFα-mediated signaling via its interaction with progranulin. Full article
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