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Trends Cell Biol. 2014 Oct;24(10):584-93. doi: 10.1016/j.tcb.2014.04.007. Epub 2014 May 16.

Secretory cargo sorting at the trans-Golgi network.

Author information

1
Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
2
Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. Electronic address: vonblume@biochem.mpg.de.

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 pre-lysosomes 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 Ca(2+) ATPase, SPCA1 (secretory pathway calcium ATPase 1), and the luminal 45 kDa Ca(2+)-binding protein, Cab45, for successful sorting of a subset of proteins at the TGN. We review progress in understanding these processes.

KEYWORDS:

Ca(2+); TGN; protein sorting; secretory cargo

PMID:
24841758
DOI:
10.1016/j.tcb.2014.04.007
[Indexed for MEDLINE]

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