A predicted α-helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway

被引:38
作者
Jutras, I
Seidah, NG
Reudelhuber, TL
机构
[1] Inst Rech Clin Montreal, Lab Mol Biochem Hypertens, Montreal, PQ H2W 1R7, Canada
[2] Inst Rech Clin Montreal, Biochem Neuroendocrinol Lab, Montreal, PQ H2W 1R7, Canada
关键词
D O I
10.1074/jbc.M004757200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The proprotein convertase PC1 is a protease whose activity is largely confined to the dense core secretory granules of neuroendocrine cells. Efficient processing of PC1 substrates in granules requires a mechanism that will both limit the activity of the enzyme to these organelles and promote its targeting to the nascent secretory granules. In the current study, we provide evidence that targeting of PC1 to secretory granules is mediated by alpha -helical structures in its C-terminal tail and, at least in part, is dependent on interactions with specific components of the secretory granule membrane.
引用
收藏
页码:40337 / 40343
页数:7
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