Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation
| Autor: | Huaxiong Qi, Duanqing Pei, Tie-Bang Kang |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Glycosylation
Amino Acid Motifs Molecular Sequence Data Golgi Apparatus Biology Matrix metalloproteinase Protein Sorting Signals Cleavage (embryo) Endoplasmic Reticulum Biochemistry Zymogen Animals Secretion Amino Acid Sequence Molecular Biology Secretory pathway Cell Nucleus Membrane Proteins Metalloendopeptidases Cell Biology Proprotein convertase Transmembrane protein Matrix Metalloproteinases Cell biology Molecular Weight Transmembrane domain COS Cells |
| Zdroj: | The Journal of biological chemistry. 275(43) |
| ISSN: | 0021-9258 |
| Popis: | Matrix metalloproteinases characterized so far are either secreted or membrane anchored via a type I transmembrane domain or a glycosylphosphatidylinositol linkage. Lacking either membrane-anchoring mechanism, the newly discovered CA-MMP/MMP-23 was reported to be expressed as a cell-associated protein. In this report, we present evidence that CA-MMP is expressed as an integral membrane zymogen with an N-terminal signal anchor, and secreted as a fully processed mature enzyme. We further demonstrate that L(20)GAALSGLCLLSALALL(36) is required for this unique membrane localization as a signal anchor and its secretion is regulated by a proprotein convertase motif RRRR(79) sandwiched between its pro- and catalytic domains. Thus, CA-MMP is a type II transmembrane MMP that can be regulated by a single proteolytic cleavage for both activation and secretion, establishing a novel paradigm for protein trafficking and processing within the secretory pathway. |
| Databáze: | OpenAIRE |
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