RRC ID |
58257
|
著者 |
Nagahama M, Taniguchi T, Hashimoto E, Imamaki A, Mori K, Tsuji A, Matsuda Y.
|
タイトル |
Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4).
|
ジャーナル |
FEBS Lett
|
Abstract |
SPC4 (PACE4), a member of the eukaryotic family of subtilisin-like proprotein convertases, is synthesized as a proenzyme (proSPC4) which undergoes proteolytic removal of N-terminal propeptide during transit through the secretory pathway. As this propeptide processing seems to be a key event in the functional expression of SPC4, we have investigated its mechanism and the intracellular site where it occurs. In transfected fibroblast cells, the 110-kDa proSPC4 undergoes slow cleavage to generate a 103-kDa mature enzyme in the endoplasmic reticulum (ER). Site-directed mutagenesis studies demonstrate that the proteolytic activation of SPC4 occurs mainly through a unimolecular autocatalytic process and propeptide cleavage is a prerequisite for its export from the ER. Sedimentation velocity and chemical cross-linking analysis demonstrate that the precursor protein in the cells exists as both a monomer and a dimer-sized complex whereas mature SPC4 exists only as a monomer. These results suggest that the cleavage of the N-terminal propeptide of SPC4 plays a regulatory role in its activation and secretion through the change in its oligomeric state.
|
巻・号 |
434(1-2)
|
ページ |
155-9
|
公開日 |
1998-8-28
|
DOI |
10.1016/s0014-5793(98)00970-3
|
PII |
S0014-5793(98)00970-3
|
PMID |
9738469
|
MeSH |
Animals
Cell Line
Humans
Isoenzymes / biosynthesis*
Isoenzymes / chemistry
Proprotein Convertases
Protein Conformation*
Protein Processing, Post-Translational
Serine Endopeptidases / biosynthesis*
Serine Endopeptidases / chemistry
|
IF |
3.057
|
引用数 |
27
|
リソース情報 |
遺伝子材料 |
Human PACE4 cDNA (RDB02938) |