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Trends Cell Biol. 2016 May;26(5):379-388. doi: 10.1016/j.tcb.2015.12.004. Epub 2016 Jan 29.

Cracking the Glycome Encoder: Signaling, Trafficking, and Glycosylation.

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Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, 138673 Singapore; Department of Biochemistry, National University of Singapore, 21 Lower Kent Ridge Road, 119077 Singapore. Electronic address:
Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, 138673 Singapore.


The glycoproteome, the ensemble of glycans and their carrier proteins, plays major roles in multicellular life by regulating cell interactions with their environment. How information is encoded into the glycome, in other words how glycosylation is modulated in response to signals, remains largely unclear. Glycosylation enzymes operate predominantly in the endoplasmic reticulum (ER) and Golgi, a highly compartmentalized membrane-bound environment. Recent work indicates that this compartmentalization is plastic and tightly regulated. For instance, specific signals can induce the relocation of O-glycosylation enzymes, GALNTs, from the Golgi to the ER, resulting in significant upregulation of O-glycosylation initiation. We have named this re-compartmentation process the 'GALA pathway'. GALA illustrates how membrane trafficking in the secretory pathway can regulate protein glycosylation and thus encode information in the glycome.


GALNT; Golgi; cancer; glycosylation; invasion; membrane trafficking

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