期刊
TRENDS IN CELL BIOLOGY
卷 24, 期 10, 页码 584-593出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2014.04.007
关键词
Ca2+; TGN; protein sorting; secretory cargo
类别
资金
- Emmy Noether fellowship from the Deutsche Forschungsgemeinschaft (DFG) [BL 1186/1-1]
- European Commission Framework Program (FP7) Marie Curie Career Reintegration grant
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.
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