Journal
TRAFFIC
Volume 24, Issue 1, Pages 4-19Publisher
WILEY
DOI: 10.1111/tra.12873
Keywords
Cab45; lysosomal hydrolases; progranulin; prosaposin; TGN export
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The Golgi resident protein Cab45 plays a significant role in the sorting of secretory cargo at the trans-Golgi Network (TGN). Cab45 oligomerizes upon Ca2+ influx and recruits and packages soluble cargo molecules into transport carriers. This research discovered a new function of Cab45 in lysosomal function regulation.
The trans-Golgi Network (TGN) sorts molecular addresses and sends newly synthesized proteins to their destination via vesicular transport carriers. Despite the functional significance of packaging processes at the TGN, the sorting of soluble proteins remains poorly understood. Recent research has shown that the Golgi resident protein Cab45 is a significant regulator of secretory cargo sorting at the TGN. Cab45 oligomerizes upon transient Ca2+ influx, recruits soluble cargo molecules (clients), and packs them in sphingomyelin-rich transport carriers. However, the identity of client molecules packed into Cab45 vesicles is scarce. Therefore, we used a precise and highly efficient secretome analysis technology called hiSPECs. Intriguingly, we observed that Cab45 deficient cells manifest hypersecretion of lysosomal hydrolases. Specifically, Cab45 deficient cells secrete the unprocessed precursors of prosaposin (PSAP) and progranulin (PGRN). In addition, lysosomes in these cells show an aberrant perinuclear accumulation suggesting a new role of Cab45 in lysosomal positioning. This work uncovers a yet unknown function of Cab45 in regulating lysosomal function.
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