Evidence for protein splicing in the endoplasmic reticulum-Golgi intermediate compartment

We present evidence that the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is a site for protein splicing of cathepsin C: (i) maturation of the enzyme in COS 7 cells is a two-step process starting within the ERGIC, and (ii) the intermediately processed polypeptide retains both termini...

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Published inBiochimica et biophysica acta Vol. 1448; no. 3; pp. 507 - 511
Main Authors Demirov, D., Sarafian, V., Kremensky, I., Ganev, V.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 11.01.1999
Subjects
Animals
Binding Sites - genetics
Cathepsin C
Cell Compartmentation
COS Cells
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism
Endoplasmic Reticulum - metabolism
Endoplasmic reticulum-Golgi intermediate compartment
Enzyme Precursors - genetics
Enzyme Precursors - metabolism
Glycosylation
Golgi Apparatus - metabolism
Mutagenesis, Site-Directed
Protein Processing, Post-Translational
Protein sorting
Protein splicing
Proteins - metabolism
Rats
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Transfection
Protein splicing
Endoplasmic reticulum-Golgi intermediate compartment
Protein sorting
Cathepsin C
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Summary:We present evidence that the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is a site for protein splicing of cathepsin C: (i) maturation of the enzyme in COS 7 cells is a two-step process starting within the ERGIC, and (ii) the intermediately processed polypeptide retains both termini of the proenzyme and lacks an internal fragment.
ISSN:0167-4889
0006-3002
1879-2596
1878-2434
DOI:10.1016/S0167-4889(98)00158-X