AI Article Synopsis
- Membrane-bound mucins are large O-glycoproteins linked to various cancers and inflammatory diseases, and they can interact with the ErbB2 receptor, impacting cancer outcomes.
- The paper highlights that mucins MUC3, MUC4, MUC12, MUC13, and MUC17 share an evolutionary origin and similar structural features, particularly EGF-like and SEA domains.
- The study analyzes the structure-function relationships of these mucins, suggesting they have shared biological roles and discusses the potential for targeting ErbB2-related pathways in cancer therapies.
Article Abstract
Membrane-bound mucins belong to a heterogeneous family of large O-glycoproteins involved in numerous cancers and inflammatory diseases of the epithelium. Some of them are also involved in protein-protein interactions, with receptor tyrosine kinase ErbB2, and fundamental and clinical data showed that these complexes have a detrimental impact on cancer outcome, thus raising interest in therapeutic targeting. This paper aims to demonstrate that MUC3, MUC4, MUC12, MUC13, and MUC17 have a common evolutionary origin and share a common structural organization with EGF-like and SEA domains. Theoretical structure-function relationship analysis of the conserved domains indicated that the studied membrane-bound mucins share common biological properties along with potential specific functions. Finally, the potential druggability of these complexes is discussed, revealing ErbB2-related pathways of cell signaling to be targeted.
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| http://dx.doi.org/10.1021/acs.jmedchem.9b02001 | DOI Listing |
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