{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n The conserved oligomeric Golgi (COG) complex is essential for proper intra‐Golgi vesicle tethering, glycosylation, and overall Golgi homeostasis. In particular, COG8, one of its eight subunits, plays a pivotal role in assembling the complete COG complex by bridging the two subcomplexes (lobe A and lobe B). Studies have demonstrated that loss‐of‐function mutations in COG8 lead to a type II congenital disorder of glycosylation (CDG‐IIh) characterized by defects in terminal glycan sialylation and a broad spectrum of neurologic and systemic abnormalities."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Detailed analyses of COG complex organization show that COG8 stably associates with both the Cog1–4 and Cog5–7 subcomplexes, thereby mediating their integration into a functional tethering machinery critical for Golgi dynamics."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Beyond its classical role in glycosylation, COG8 functions in several other cellular processes. Its interaction with an atypical calcineurin variant (CnAβ1) at the Golgi links COG8 to mTORC2 signaling pathways that are essential for mesoderm specification during embryonic stem cell differentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " In addition, specific silencing of COG8 in human cells has been shown to impair HIV-1 replication and, more recently, genome-wide screens have identified COG8 as a key host factor required for SARS-CoV-2 infection by regulating viral protein transport and immune factor expression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Moreover, in yeast the Arl3–Arl1 GTPase cascade cooperates with COG8 to modulate selective autophagy through regulation of Atg9 trafficking."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Finally, chimeric transcripts involving COG8 (for instance, a TMED6–COG8 read-through chimera) have been observed in TFE3 translocation renal cell carcinomas and may hold promise as diagnostic markers."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Collectively, these findings underscore that COG8 is not only critical for the structural integrity and function of the Golgi apparatus through its role in vesicle tethering and glycosylation, but it also participates in diverse processes including signal transduction, selective autophagy, and host–pathogen interactions.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christian Kranz, Bobby G Ng, Liangwu Sun, et al. 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