Ankyrin is a target of spectrin's E2/E3 ubiquitin-conjugating/ligating activity.
Cell Mol Biol (Noisy-le-grand)
; 50(1): 59-66, 2004 Feb.
Article
en En
| MEDLINE
| ID: mdl-15040428
Ubiquitin is a small protein of 8.6 kDa molecular weight. When polyubiquitin is attached to target proteins, they are tagged for destruction by cytoplasmic organelles called proteasomes. We now know that ubiquitination of target proteins also regulates functions as diverse as the sorting of proteins to different intracellular destinations, cell signaling, cell division, gene transcription, and protein-protein interactions. The ubiquitination of target proteins requires a cascade of enzymes: E1 ubiquitin activating enzyme, E2 ubiquitin conjugating enzyme and E3 ubiquitin ligating enzyme. Recently we have demonstrated that the red blood cell (RBC) membrane skeletal protein, spectrin, has E2/E3 enzymatic activities in its alpha-subunit, that can transfer ubiquitin to itself. We have now created a cell free assay using biotinylated ubiquitin that allows detection of target proteins by streptavidin peroxidase. This approach coupled with immunoprecipitation, purification and micro liquid chromatography coupled to tandem mass spectrometry has identified ankyrin as a target of spectrin's E2/E3 activity. Western blotting, with ubiquitin antibody, of purified ankyrin and its well characterized functional domains, has demonstrated that both the spectrin and band 3 binding domains are ubiquitinated in vivo.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ubiquitinas
/
Espectrina
/
Ancirinas
/
Enzimas Ubiquitina-Conjugadoras
Límite:
Humans
Idioma:
En
Revista:
Cell Mol Biol (Noisy-le-grand)
Año:
2004
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Francia