Functional Roles of Protein O-Glycosylation
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".
Deadline for manuscript submissions: closed (15 September 2018) | Viewed by 38554
Special Issue Editors
Interests: mucin-type O-glycosylation; O-glycoproteins; mucins; MUC1; cancer; innate immunity; galactosemia; glycomics; (glyco)proteomics; mass spectrometry
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Complex glycosylation of proteins comprizing O- and N-linked glycan chains represents a high-impact topic in current biological research and, in particular, in human life sciences. In this Special Issue, we undertake the attempt to collect contributions that cover at least part of this huge and still-growing field by restriction to the functional roles of protein O-glycosylation. No focus on a particular subtype is envisaged, e.g., the abundant mucin-type forms (O-GalNAc) or the more rare types of O-glycosylation, such as O-Man, O-Fuc, or O-Glc. Mucin-type O-glycans on mucins or mucin-like glycoproteins express ABH and Lewis blood group antigens on epithelia with impact in cancer diagnosis or as entry targets in microbial infection. Functional aspects of other types of O-glycosylation were revealed in congenital disorders of glycosylation (dystro glycanopathies) and in epithelial cell adhesion mediated by E-cadherin (O-Man). In addition to the well established involvement of O-Fuc glycosylation in notch signaling, the terminal LacdiNAc modification of extracellular matrix glycoproteins might play roles in the regulatory control of stem cell renewal.
Prof. Dr. Franz-Georg HanischDr. Isabelle Breloy
Guest Editors
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Keywords
- O-glycosylation
- membrane organization
- cellular trafficking
- cell-cell binding
- cell-matrix binding
- innate immunity
- immunology
- cancer
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