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Special Issue "Protein Glycosylation in the Secretory Pathway: Variation, Biosynthesis and Function"
Deadline for manuscript submissions: 31 December 2019.
Interests: protein glycosylation; glycoproteins; glycosyltransferases; O-mannosyl glycans; endoplasmic reticulum
In the postgenomic and proteomic era, it is becoming increasingly clear that we cannot fully understand basic cell biology as well as the growth and development of complex multicellular organisms by exploring proteins, without considering the many possible modifications. Proteins that enter and pass through the secretory pathway receive glycans, a highly diverse, complex, and energy-demanding post-translational modification. More than nine different monosaccharides, which are either N-, O- or C-glycosidically linked to the polypeptide chain, already reflect the complexity of protein glycosylation. Protein-bound sugar moieties may be further extended by highly organized reactions, ultimately leading to a glycoproteome of immense variety and information content that is cell type-specific and may even vary depending on the condition of the cell (e.g., inflammation).
Recent glycoproteomic and glycomic studies have clearly shown that the vast majority of proteins entering the secretory pathway are glycosylated. The glycan structures and glycosylation pattern are dynamically and differentially regulated during development as well as under certain pathological conditions. Glycosciences are undoubtedly experiencing a boom, as it is becoming more and more apparent that glycoproteins affect virtually all aspects of growth and development in the health and disease processes of eukaryotes.
This Special Issue will cover a broad range of studies on diversity, biosynthesis, and the function of protein glycosylation in eukaryotes ranging from yeast to human disease models. Experimental papers, recent review articles, and commentaries are welcome.
Prof. Dr. Sabine Strahl
Prof. Dr. Bernd Lepenies
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.
- Membrane protein
- Lipid linked oligosaccharide
- Sugar nucleotide transport
- Endoplasmic reticulum
- Golgi apparatus
- ER protein quality control
- ER associated protein degradation
- Protein maturation
- Cellular trafficking
- Cell–cell interaction
- Cell–matrix interaction
- Congenital disorders of glycosylation
- Fungal pathogenicity
- Innate immunity
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.
Mucosal glycosylation as a molecular player in colitis-associated colorectal cancer
Colitis-associated Cancer (CAC) is a major complication of Ulcerative Colitis remaining an important clinical challenge in terms of diagnosis and prognosis. Dysregulation of mucosal glycosylation has been described as a key regulatory mechanism associated with colon inflammation and with colorectal cancer development. In this review, we discuss the major molecular drivers of CAC pathogenesis, highlighting the role of glycans in the regulation of intestinal inflammation and its progression to CAC.
Structure and function of glycosyltransferases involved in N-glycan maturation
Masamichi Nagae, Yasuhiko Kizuka, Naoyuki Taniguchi and Yoshiki Yamaguchi
Short abstract: Glycosylation is the most ubiquitous post translational modifications in eukaryotes. N-glycan is attached to nascent glycoprotein and processed and matured by various glycosidases and glycosyltransferases during protein transport. Alternations of N-glycan structure play crucial roles in various physiological and pathological events including cancer progression. Especially, the formation of N-glycan branches catalyzed by specific N-acetylglucosaminyltransferases such as GnT-III, GnT-IVs, GnT-V, and GnT-IX and a fucosyltransferase, FUT8, regulates the functions of target glycoproteins. Recent progresses of structural analysis on these glycosyltransferases have provided insights into substrate recognition and catalytic reaction mechanisms. In this review, the structure-function relationships of these enzymes are discussed.