To cut or not to cut: New rules for proteolytic shedding of membrane proteins
| Autor: | Stefan F. Lichtenthaler, Edgar Meinl |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Proteases metabolism [Amino Acids] ADAM17 Protein Biochemistry metabolism [Cell Membrane] metabolism [ADAM17 Protein] 03 medical and health sciences Extracellular ddc:610 Amino Acids Molecular Biology chemistry.chemical_classification Metalloproteinase 030102 biochemistry & molecular biology Chemistry Cell Membrane Membrane Proteins Cell Biology Sheddase Amino acid Cell biology genetics [Membrane Proteins] ADAM Proteins 030104 developmental biology Membrane protein Ectodomain metabolism [ADAM Proteins] Proteolysis metabolism [Membrane Proteins] Function (biology) |
| Zdroj: | Journal of Biological Chemistry JBC papers in press 295(35), 12353-12354 (2020). doi:10.1074/jbc.H120.015304 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.H120.015304 |
| Popis: | Sheddases are specialized proteases that control the abundance and function of membrane proteins by cleaving their substrate's extracellular domain (ectodomain), a process known as shedding. Hundreds of shedding substrates have been identified, but little is known about the mechanisms that govern ectodomain shedding. Iwagishi et al. now report that negatively charged amino acids in the membrane-proximal juxtamembrane domain of substrates make them resistant to shedding by the metalloprotease ADAM17. These findings will help researchers better understand the regulation of shedding and may aid in the development of drugs targeting sheddases. |
| Databáze: | OpenAIRE |
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