| Autor: |
Saftig, Paul, Knecht, Erwin, Salvador, Natalia |
| Zdroj: |
Lysosomes; 2005, p181-193, 13p |
| Abstrakt: |
Many lysosomal and nonlysosomal pathways degrade intracellular proteins and this variety allows all cell proteins to be proteolysed at various speeds in response to different stimuli. Lysosomes, which are present in almost all eukaryotic cells, are major sites of intracellular proteolysis. They are quite heterogeneous and participate in protein catabolism by several mechanisms. By chaperone-mediated autophagy, lysosomes selectively degrade proteins with KFERQ-like sequences (about 25-30% of all cell proteins) by a mechanism which resembles the transport of proteins into mitochondria and other organelles since it requires (a) protein receptor(s), cytosolic and lysosomal chaperones and ATP-Mg++. This pathway appears to be only active in certain cells under specific conditions, but its quantitative importance in protein turnover, in comparison to other lysosomal and nonlysosomal pathways, is still unknown. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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