Special Issue "Signal Transduction 2016"

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (30 November 2016)

Special Issue Editor

Guest Editor
Prof. Dr. Ritva Tikkanen

Institute of Biochemistry, Medical Faculty, Justus-Liebig University of Giessen, Friedrichstrasse 24, D-35392, Giessen, Germany
Website | E-Mail
Interests: signal transduction; receptor tyrosine kinases; mitogen-activated protein kinases; endosomal sorting; lysosome biogenesis; lysosomal storage diseases; cell adhesion; cell polarity

Special Issue Information

Dear Colleagues,

Signal transduction processes are of vital importance for the cell as they regulate a plethora of cellular processes, including growth, differentiation, and cell death. The importance of cellular signaling is highlighted by the fact that signaling errors, e.g., after a mutation of endogenous genes or upon impaired stimuli, are the reason for numerous human diseases. However, although signaling cascades are frequently depicted as linear “flow-charts”, the cellular reality is much more complicated, and the signaling pathways frequently crosstalk and interact. Thus, understanding the fine-tuning of signaling, and the networks of signaling molecules, will be a major task in the future. In this Special Issue, we are interested in manuscripts (e.g., reviews or original articles) that address various aspects of this important topic. We especially welcome manuscripts that focus on aberrant signaling, such as oncogenic signal transduction and networks, or crosstalk between signaling pathways. However, manuscripts about signaling in normal cells are also highly appreciated. We hope that this important topic will attract a large number of contributions from both basic and clinical scientists.

Prof. Dr. Ritva Tikkanen
Guest Editor

Manuscript Submission Information

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Keywords

  • signal transduction
  • receptors
  • hormones, growth factors
  • phosphorylation
  • ubiquitin
  • spatial and temporal signaling
  • differentiation and growth
  • cancer
  • signaling networks
  • crosstalk and transactivation

Published Papers (5 papers)

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Research

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Open AccessFeature PaperArticle Random Splicing of Several Exons Caused by a Single Base Change in the Target Exon of CRISPR/Cas9 Mediated Gene Knockout
Cells 2016, 5(4), 45; doi:10.3390/cells5040045
Received: 20 October 2016 / Revised: 3 December 2016 / Accepted: 9 December 2016 / Published: 14 December 2016
Cited by 5 | PDF Full-text (3608 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The clustered regularly interspaced short palindromic repeats (CRISPR)-associated sequence 9 (CRISPR/Cas9) system is widely used for genome editing purposes as it facilitates an efficient knockout of a specific gene in, e.g. cultured cells. Targeted double-strand breaks are introduced to the target sequence of
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The clustered regularly interspaced short palindromic repeats (CRISPR)-associated sequence 9 (CRISPR/Cas9) system is widely used for genome editing purposes as it facilitates an efficient knockout of a specific gene in, e.g. cultured cells. Targeted double-strand breaks are introduced to the target sequence of the guide RNAs, which activates the cellular DNA repair mechanism for non-homologous-end-joining, resulting in unprecise repair and introduction of small deletions or insertions. Due to this, sequence alterations in the coding region of the target gene frequently cause frame-shift mutations, facilitating degradation of the mRNA. We here show that such CRISPR/Cas9-mediated alterations in the target exon may also result in altered splicing of the respective pre-mRNA, most likely due to mutations of splice-regulatory sequences. Using the human FLOT-1 gene as an example, we demonstrate that such altered splicing products also give rise to aberrant protein products. These may potentially function as dominant-negative proteins and thus interfere with the interpretation of the data generated with these cell lines. Since most researchers only control the consequences of CRISPR knockout at genomic and protein level, our data should encourage to also check the alterations at the mRNA level. Full article
(This article belongs to the Special Issue Signal Transduction 2016)
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Review

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Open AccessReview Invariant Chain Complexes and Clusters as Platforms for MIF Signaling
Cells 2017, 6(1), 6; doi:10.3390/cells6010006
Received: 8 December 2016 / Revised: 5 February 2017 / Accepted: 7 February 2017 / Published: 10 February 2017
Cited by 1 | PDF Full-text (4420 KB) | HTML Full-text | XML Full-text
Abstract
Invariant chain (Ii/CD74) has been identified as a surface receptor for migration inhibitory factor (MIF). Most cells that express Ii also synthesize major histocompatibility complex class II (MHC II) molecules, which depend on Ii as a chaperone and a targeting factor. The assembly
[...] Read more.
Invariant chain (Ii/CD74) has been identified as a surface receptor for migration inhibitory factor (MIF). Most cells that express Ii also synthesize major histocompatibility complex class II (MHC II) molecules, which depend on Ii as a chaperone and a targeting factor. The assembly of nonameric complexes consisting of one Ii trimer and three MHC II molecules (each of which is a heterodimer) has been regarded as a prerequisite for efficient delivery to the cell surface. Due to rapid endocytosis, however, only low levels of Ii-MHC II complexes are displayed on the cell surface of professional antigen presenting cells and very little free Ii trimers. The association of Ii and MHC II has been reported to block the interaction with MIF, thus questioning the role of surface Ii as a receptor for MIF on MHC II-expressing cells. Recent work offers a potential solution to this conundrum: Many Ii-complexes at the cell surface appear to be under-saturated with MHC II, leaving unoccupied Ii subunits as potential binding sites for MIF. Some of this work also sheds light on novel aspects of signal transduction by Ii-bound MIF in B-lymphocytes: membrane raft association of Ii-MHC II complexes enables MIF to target Ii-MHC II to antigen-clustered B-cell-receptors (BCR) and to foster BCR-driven signaling and intracellular trafficking. Full article
(This article belongs to the Special Issue Signal Transduction 2016)
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Open AccessReview Role of Cytokine-Induced Glycosylation Changes in Regulating Cell Interactions and Cell Signaling in Inflammatory Diseases and Cancer
Cells 2016, 5(4), 43; doi:10.3390/cells5040043
Received: 14 October 2016 / Revised: 23 November 2016 / Accepted: 24 November 2016 / Published: 29 November 2016
Cited by 13 | PDF Full-text (2479 KB) | HTML Full-text | XML Full-text
Abstract
Glycosylation is one of the most important modifications of proteins and lipids, and cell surface glycoconjugates are thought to play important roles in a variety of biological functions including cell-cell and cell-substrate interactions, bacterial adhesion, cell immunogenicity and cell signaling. Alterations of glycosylation
[...] Read more.
Glycosylation is one of the most important modifications of proteins and lipids, and cell surface glycoconjugates are thought to play important roles in a variety of biological functions including cell-cell and cell-substrate interactions, bacterial adhesion, cell immunogenicity and cell signaling. Alterations of glycosylation are observed in number of diseases such as cancer and chronic inflammation. In that context, pro-inflammatory cytokines have been shown to modulate cell surface glycosylation by regulating the expression of glycosyltransferases involved in the biosynthesis of carbohydrate chains. These changes in cell surface glycosylation are also known to regulate cell signaling and could contribute to disease pathogenesis. This review summarizes our current knowledge of the glycosylation changes induced by pro-inflammatory cytokines, with a particular focus on cancer and cystic fibrosis, and their consequences on cell interactions and signaling. Full article
(This article belongs to the Special Issue Signal Transduction 2016)
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Open AccessReview Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
Cells 2016, 5(1), 4; doi:10.3390/cells5010004
Received: 11 December 2015 / Revised: 20 January 2016 / Accepted: 20 January 2016 / Published: 25 January 2016
Cited by 2 | PDF Full-text (1197 KB) | HTML Full-text | XML Full-text
Abstract
In response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abundance of target mRNAs,
[...] Read more.
In response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abundance of target mRNAs, and affect gene expression during cellular activation, proliferation, and stress responses. In this review, we summarize the effect of phosphorylation on the function of ARE-binding proteins ZFP36 and ELAVL1 and the GRE-binding protein CELF1. The networks of target mRNAs that these proteins bind and regulate include transcripts encoding kinases and kinase signaling pathways (KSP) components. Thus, kinase signaling pathways are involved in feedback regulation, whereby kinases regulate RNA-binding proteins that subsequently regulate mRNA stability of ARE- or GRE-containing transcripts that encode components of KSP. Full article
(This article belongs to the Special Issue Signal Transduction 2016)
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Open AccessReview Re-Use of Established Drugs for Anti-Metastatic Indications
Cells 2016, 5(1), 2; doi:10.3390/cells5010002
Received: 21 November 2015 / Revised: 4 January 2016 / Accepted: 8 January 2016 / Published: 12 January 2016
Cited by 3 | PDF Full-text (523 KB) | HTML Full-text | XML Full-text
Abstract
Most patients that die from cancer do not die due to the primary tumor but due to the development of metastases. However, there is currently still no drug on the market that specifically addresses and inhibits metastasis formation. This lack was, in the
[...] Read more.
Most patients that die from cancer do not die due to the primary tumor but due to the development of metastases. However, there is currently still no drug on the market that specifically addresses and inhibits metastasis formation. This lack was, in the past, largely due to the lack of appropriate screening models, but recent developments have established such models and have provided evidence that tumor cell migration works as a surrogate for metastasis formation. Herein we deliver on several examples a rationale for not only testing novel cancer drugs by use of these screening assays, but also reconsider established drugs even of other fields of indication. Full article
(This article belongs to the Special Issue Signal Transduction 2016)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of the paper: Review
Tentative title: The Diverse Functions and Signal Transduction of the Exocyst Complex in Tumor Cells
Authors: Toshiaki Tanaka 1,2,*, Kaoru Goto 1, Mitsuyoshi Iino 2
Affiliations: 1 Department of Anatomy and Cell Biology, School of Medicine, Yamagata University, 2-2-2 Iidanishi, Yamagata, Japan; 2 Department of Dentistry, Oral and Maxillofacial Surgery, Plastic and Reconstructive Surgery, School of Medicine, Yamagata University, 2-2-2 Iidanishi, Yamagata, Japan; * Corresponding author.
Abstract: The exocyst complexes are the large conserved hetero-oligomeric complexes that consist of Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70, and Exo84.The exocyst complexes are implicated in the targeting of vesicles for regulated exocytosis in various cell types and important for targeted exocytosis of post-Golgi transport vesicles to the plasma membrane. The exocyst complexes are essential for membrane growth and secretion and function in exocytosis, endocytosis, cytokinesis, and autophagy. Therefore, recent studies indicated that the exocyst complexes may be involved in several diseases such as Meckel-Gruber syndrome, neuropathogenesis, diabetes, and cancers.In this review, we focus on the diverse functions and cellular signaling pathways in various tumors.

Tentative title: Role of Cytokines-Induced Glycosylation Changes in Regulating Cell Interactions and Cell Signaling
Authors: Justine H. Dewald, Florent Colomb, Marie Bobowski, Sophie Groux-Degroote, Philippe Delannoy
Abstract: Glycosylation is one of the most important modifications of proteins and lipids, and cell surface glycoconjugates are thought to play important roles in a variety of biological functions including cell–cell and cell-substrate interactions, bacterial adhesion, cell immunogenicity and cell signaling. Glycosylation alterations are observed in several diseases such as cancer and chronic inflammation. In that context, pro-inflammatory cytokines have been shown to regulate cell surface glycosylation by regulating the expression of glycosyltransferases involved in the biosynthesis of carbohydrate chains. These changes in cell surface glycosylation are also known to regulate cell signaling and could contribute to disease pathogenesis. This review summarizes our current knowledge of the glycosylation changes induced by pro-inflammatory cytokines, with a particular focus on cancer and chronic inflammation, and their consequences on cell interactions and signaling.

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