Literature DB >> 26832820

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

Frederic Bard1, Joanne Chia2.   

Abstract

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.
Copyright © 2015 Elsevier Ltd. All rights reserved.

Entities:  

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

Mesh:

Substances:

Year:  2016        PMID: 26832820     DOI: 10.1016/j.tcb.2015.12.004

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  24 in total

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8.  Giantin-knockout models reveal a feedback loop between Golgi function and glycosyltransferase expression.

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Journal:  Nat Commun       Date:  2021-07-01       Impact factor: 14.919

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