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Tyrosine phosphorylation directs TACE into extracellular vesicles via unconventional secretion.

Traffic 2018 December 21
When studying how HIV-1 Nef can promote packaging of the proinflammatory transmembrane protease TACE into extracellular vesicles (EV) we have revealed a novel tyrosine kinase-regulated unconventional protein secretion (UPS) pathway for TACE. When TACE was expressed without its trafficking co-factor iRhom allosteric Hck activation by Nef triggered translocation of TACE into EVs. This process was insensitive to blocking of classical secretion by inhibiting ER to Golgi transport, and involved a distinct form of TACE devoid of normal glycosylation and incompletely processed for prodomain removal. Like most other examples of UPS this process was GRASP-dependent but was not associated with ER stress. These data indicate that Hck-activated UPS provides an alternative pathway for TACE secretion that can bypass iRhom-dependent ER to Golgi transfer, and suggest that tyrosine phosphorylation might have a more general role in regulating UPS. This article is protected by copyright. All rights reserved.

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