Evidence for proprotein convertase activity in the endoplasmic reticulum/early Golgi

被引：29
作者：
Salvas, A
Benjannet, S
Reudelhuber, TL
Chrétien, M
Seidah, NG
机构：
[1] Clin Res Inst Montreal, Biochem Neuroendocrinol Lab, Montreal, PQ H2W 1R7, Canada
[2] Clin Res Inst Montreal, Lab Mol Biol Hypertens, Montreal, PQ H2W 1R7, Canada
[3] Ottawa Hlth Res Inst, Reg Prot Chem Ctr, Dis Ageing Unit, Ottawa, ON K1Y 4E9, Canada
来源：
FEBS LETTERS | 2005年 / 579卷 / 25期
基金：
加拿大健康研究院;
关键词：
proprotein convertase; furin; PC7; PC1; prosegment; endoplasmic reticulum;
D O I：
10.1016/j.febslet.2005.09.029
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：
Processing of precursor proteins by the proprotein convertases is thought to occur mainly in the trans-Golgi network or post-Golgi compartments. Such cleavage is inhibited by the prosegment of the convertases. During our studies of the use of the inhibitory prosegment of PC1, we noticed that a construct containing the prosegment fused to the C-terminal secretory granule sorting domain was cleaved in the endoplasmic reticulum (ER) at a pair of basic residues, best recognized by furin and PC7. This was further confirmed when this construct was fused at the C-terminus with a KDEL ER-retention signal. This suggests that the convertases could cleave some substrates within the ER, possibly by displacing the inhibitory prosegment associated with them. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码：5621 / 5625
页数：5
相关论文
共 24 条
[11]   Prohormone convertase 1 (PC1) processing and sorting: effect of PC1 propeptide and proSAAS [J].
Lee, SN ;
Prodhomme, E ;
Lindberg, I .
JOURNAL OF ENDOCRINOLOGY, 2004, 182 (02) :353-364
[12]   BREFELDIN-AS EFFECTS ON ENDOSOMES, LYSOSOMES, AND THE TGN SUGGEST A GENERAL MECHANISM FOR REGULATING ORGANELLE STRUCTURE AND MEMBRANE TRAFFIC [J].
LIPPINCOTTSCHWARTZ, J ;
YUAN, L ;
TIPPER, C ;
AMHERDT, M ;
ORCI, L ;
KLAUSNER, RD .
CELL, 1991, 67 (03) :601-616
[13]   Neuroendocrine secretory protein 7B2:: structure, expression and functions [J].
Mbikay, M ;
Seidah, NG ;
Chrétien, M .
BIOCHEMICAL JOURNAL, 2001, 357 :329-342
[14]   A C-TERMINAL SIGNAL PREVENTS SECRETION OF LUMINAL ER PROTEINS [J].
MUNRO, S ;
PELHAM, HRB .
CELL, 1987, 48 (05) :899-907
[15]   The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1 [J].
Qian, YM ;
Devi, LA ;
Mzhavia, N ;
Munzer, S ;
Seidah, NG ;
Fricker, LD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (31) :23596-23601
[16]   Purification and characterization of the human KDEL receptor [J].
Scheel, AA ;
Pelham, HRB .
BIOCHEMISTRY, 1996, 35 (31) :10203-10209
[17]   Precursor convertases in the secretory pathway, cytosol and extracellular milieu [J].
Seidah, NG ;
Prat, A .
PROTEASES IN BIOLOGY AND MEDICINE, 2002, 38 :79-94
[18]   Proprotein and prohormone convertases:: a family of subtilases generating diverse bioactive polypeptides [J].
Seidah, NG ;
Chrétien, M .
BRAIN RESEARCH, 1999, 848 (1-2) :45-62
[19]   CLONING AND PRIMARY SEQUENCE OF A MOUSE CANDIDATE PROHORMONE CONVERTASE PC1 HOMOLOGOUS TO PC2, FURIN, AND KEX2 - DISTINCT CHROMOSOMAL LOCALIZATION AND MESSENGER-RNA DISTRIBUTION IN BRAIN AND PITUITARY COMPARED TO PC2 [J].
SEIDAH, NG ;
MARCINKIEWICZ, M ;
BENJANNET, S ;
GASPAR, L ;
BEAUBIEN, G ;
MATTEI, MG ;
LAZURE, C ;
MBIKAY, M ;
CHRETIEN, M .
MOLECULAR ENDOCRINOLOGY, 1991, 5 (01) :111-122
[20]   CDNA SEQUENCE OF 2 DISTINCT PITUITARY PROTEINS HOMOLOGOUS TO KEX2 AND FURIN GENE-PRODUCTS - TISSUE-SPECIFIC MESSENGER-RNAS ENCODING CANDIDATES FOR PRO-HORMONE PROCESSING PROTEINASES [J].
SEIDAH, NG ;
GASPAR, L ;
MION, P ;
MARCINKIEWICZ, M ;
MBIKAY, M ;
CHRETIEN, M .
DNA AND CELL BIOLOGY, 1990, 9 (06) :415-424
123