Cdc48/Shp1 participates in dissociation of protein complexes to regulate their activity
| Autor: | Peter K. Kaiser, Linda Lauinger, Karin Flick |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Proteasome Endopeptidase Complex
0303 health sciences Saccharomyces cerevisiae Proteins biology Ubiquitin 030302 biochemistry & molecular biology Intracellular Signaling Peptides and Proteins Cell Cycle Proteins Saccharomyces cerevisiae General Medicine SCF Ubiquitin Ligase Proteomics Dissociation (chemistry) Cofactor Cell biology Ubiquitin ligase Fight-or-flight response 03 medical and health sciences Adenosine Triphosphate Valosin Containing Protein Multiprotein Complexes Genetics biology.protein Protein Binding 030304 developmental biology |
| Zdroj: | Current Genetics. 67:263-265 |
| ISSN: | 1432-0983 0172-8083 |
| DOI: | 10.1007/s00294-020-01136-1 |
| Popis: | The AAA-ATPase p97/Cdc48 is one of the most abundant proteins in eukaryotes, and owing to its multiple functions, is considered the swiss army knife of cells. Recent findings demonstrate that p97/Cdc48 and its cofactor p47/Shp1 control the heavy metal stress response by active, signal-triggered disassembly of a multisubunit ubiquitin ligase. Here we review this pathway and describe recently achieved mechanistic insight into the role of p47/Shp1 in this process. |
| Databáze: | OpenAIRE |
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