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Secretory cargo sorting at the trans-Golgi network

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Kienzle,  Christine
von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

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von Blume,  Julia
von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

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Kienzle, C., & von Blume, J. (2014). Secretory cargo sorting at the trans-Golgi network. TRENDS IN CELL BIOLOGY, 24(10), 584-593. doi:10.1016/j.tcb.2014.04.007.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-457F-5
Abstract
Sorting of proteins for secretion from cells is crucial for normal physiology and the regulation of key cellular events. Although the sorting of lysosomal hydrolases at the trans-Golgi network (TGN) for delivery to prelysosomes is well characterized, the corresponding mechanism by which secreted proteins are sorted for plasma-membrane delivery remains poorly understood. Recent discoveries have revealed a novel sorting mechanism that requires the linkage between the cytoplasmic actin cytoskeleton to the membrane-anchored Ca2+ ATPase, SPCA1 (secretory pathway calcium ATPase 1), and the luminal 45 kDa Ca2+-binding protein, Cab45, for successful sorting of a subset of proteins at the TGN. We review progress in understanding these processes.