Cracking the Glycome Encoder: Signaling, Trafficking and Glycosylation

被引:64
作者
Bard, Frederic [1 ,2 ]
Chia, Joanne [1 ]
机构
[1] Inst Mol & Cell Biol, 61 Biopolis Dr, Singapore 138673, Singapore
[2] Natl Univ Singapore, Dept Biochem, 21 Lower Kent Ridge Rd, Singapore 119077, Singapore
关键词
POLYPEPTIDE GALNAC-TRANSFERASES; FAMILIAL TUMORAL CALCINOSIS; O-GLYCOSYLATION; LECTIN DOMAINS; CELL-ADHESION; GOLGI-APPARATUS; CANCER; TN; SECRETION; ACTIVATION;
D O I
10.1016/j.tcb.2015.12.004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:379 / 388
页数:10
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