About half of the eukaryotic proteins bind biometals that participate in their structure and functions in virtually all physiological processes, including glycosylation. After reviewing the biological roles and transport mechanisms of calcium, magnesium, manganese, zinc and cobalt acting as cofactors of the metalloproteins involved in sugar metabolism and/or glycosylation, the paper will outline the pathologies resulting from a dysregulation of these metals homeostasis and more particularly Congenital Disorders of Glycosylation (CDGs) caused by ion transporter defects. Highlighting of CDGs due to defects in SLC39A8 (ZIP8) and TMEM165, two proteins transporting manganese from the extracellular space to cytosol and from cytosol to the Golgi lumen, respectively, has emphasized the importance of manganese homeostasis for glycosylation. Based on our current knowledge of TMEM165 structure and functions, this review will draw a picture of known and putative mechanisms regulating manganese homeostasis in the secretory pathway.

大约一半的真核蛋白结合生物金属，这些金属实际上参与了包括糖基化在内的所有生理过程的结构和功能。在回顾了钙，镁，锰，锌和钴作为参与糖代谢和/或糖基化的金属蛋白的辅因子的生物学作用和转运机制后，本文将概述由这些金属稳态失调所引起的病理，尤其是由离子转运蛋白缺陷引起的先天性糖基化障碍（CDG）。由于SLC39A8（ZIP8）和TMEM165中的缺陷而引起的CDG的突出显示，两种分别将锰从细胞外空间转运到细胞质和从细胞质转运到高尔基体腔的蛋白质强调了锰稳态对糖基化的重要性。