Misfolded Gβ is recruited to cytoplasmic dynein by Nudel for efficient clearance
The Gβγ heterodimer is an important signal transducer. Gβ, however, is prone to misfoiding due to its requirement for GT and chaperones for proper folding. How cells dispose of misfolded Gβ (mfGβ) is not clear. Here, we showed that mfGβ was able to be polyubiquitinated and subsequently degraded by t...
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Veröffentlicht in: | Cell research 2012-07, Vol.22 (7), p.1140-1154 |
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Sprache: | eng |
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