Person: Yang, Jia-Shu
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Yang
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Jia-Shu
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Yang, Jia-Shu
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Publication The Protein Kinase Akt Acts as a Coat Adaptor in Endocytic Recycling(Springer Science and Business Media LLC, 2020-06-15) Hsu, Jia-Wei; Bai, Ming; Li, Kunhua; Yang, Jia-Shu; Chu, Nam; Cole, Philip; Eck, Michael J.; Li, Jian; Hsu, VictorCoat proteins play a central role in vesicular transport by binding to cargoes for their sorting into intracellular pathways. Cargo recognition is mediated by components of the coat complex known as adaptor proteins. We previously showed that ACAP1 (ArfGAP with Coil-coil Ankyrin repeat Protein 1) functions as an adaptor for a clathrin coat complex acting in endocytic recycling. Here, we find that the protein kinase Akt acts as a co-adaptor in this complex, needed in conjunction with ACAP1 to bind cargo proteins for their recycling. Besides advancing the understanding of endocytic recycling, our findings uncover a fundamentally different way that a kinase acts, being an effector rather than a regulator in a cellular event.Publication Coordinated regulation of bidirectional COPI transport at the Golgi by cdc42(2015) Park, Seung-Yeol; Yang, Jia-Shu; Schmider, Angela; Soberman, Roy; Hsu, VictorThe Golgi complex plays a central role in the intracellular sorting of secretory proteins 1,2. Anterograde transport through the Golgi has been explained by the movement of Golgi cisternae, known as cisternal maturation 3–5. Because this explanation is now appreciated to be incomplete 6, interest has developed in understanding tubules that connect the Golgi cisternae 7–9. Here, we find that the Coat Protein I (COPI) complex sorts anterograde cargoes into these tubules. Moreover, the small GTPase cdc42 regulates bidirectional Golgi transport by targeting the dual functions of COPI in cargo sorting and carrier formation. Cdc42 also directly imparts membrane curvature in promoting COPI tubule formation. Our findings further reveal that COPI tubular transport complements cisternal maturation in explaining how anterograde Golgi transport is achieved, and that bidirectional COPI transport is modulated by environmental cues through cdc42.