Processing and trafficking of a prohormone convertase 2 active site mutant.

doi:10.1016/j.bbrc.2007.02.034

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Article

Processing and trafficking of a prohormone convertase 2 active site mutant.

Biochemical and biophysical research communications - 13 Apr 2007

Lee Sang-Nam, Kacprzak Magdalena M, Day Robert, Lindberg Iris

Abstract excerpt

Processing of most PC zymogens is required for successful folding and/or passage through the secretory pathway; active site mutants are retained in the ER and degraded. We here report that the active site serine mutant of PC2 (PC2-S383A) was efficiently secreted as the intact zymogen in CHO-K1 cells, suggesting that its propeptide can productively insert into the mutated binding pocket without causing misfolding....

Topics

Amino Acid Sequence
Animals
Binding Sites
CHO Cells
Cricetinae
Cricetulus
Hydrogen-Ion Concentration
Mice
Molecular Sequence Data
Mutation
Proprotein Convertase 2
Protein Folding
Protein Transport
Secretory Vesicles
Serine

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Identifiers

PMID: 17320043
DOI: 10.1016/j.bbrc.2007.02.034
PMCID: PMC2040296

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