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Biomolecules 2016, 6(3), 34;

Functional Consequences of Differential O-glycosylation of MUC1, MUC4, and MUC16 (Downstream Effects on Signaling)

Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 68198, USA
Author to whom correspondence should be addressed.
Academic Editor: Franz-Georg Hanisch
Received: 3 June 2016 / Revised: 18 July 2016 / Accepted: 21 July 2016 / Published: 30 July 2016
(This article belongs to the Special Issue Cancer and Glycosylation)
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Glycosylation is one of the most abundant post-translational modifications that occur within the cell. Under normal physiological conditions, O-linked glycosylation of extracellular proteins is critical for both structure and function. During the progression of cancer, however, the expression of aberrant and truncated glycans is commonly observed. Mucins are high molecular weight glycoproteins that contain numerous sites of O-glycosylation within their extracellular domains. Transmembrane mucins also play a functional role in monitoring the surrounding microenvironment and transducing these signals into the cell. In cancer, these mucins often take on an oncogenic role and promote a number of pro-tumorigenic effects, including pro-survival, migratory, and invasive behaviors. Within this review, we highlight both the processes involved in the expression of aberrant glycan structures on mucins, as well as the potential downstream impacts on cellular signaling. View Full-Text
Keywords: mucin; cancer; O-glycosylation; MUC1; MUC4; MUC16; signaling mucin; cancer; O-glycosylation; MUC1; MUC4; MUC16; signaling

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Hanson, R.L.; Hollingsworth, M.A. Functional Consequences of Differential O-glycosylation of MUC1, MUC4, and MUC16 (Downstream Effects on Signaling). Biomolecules 2016, 6, 34.

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