Misfolded Gβ is recruited to cytoplasmic dynein by Nudel for efficient clearance
Misfolded Gβ is recruited to cytoplasmic dynein by
Nudel for efficient clearance
Yihan Wan;Zhenye Yang;Jing Guo;Qiangge Zhang;Liyong Zeng;Wei Song;Yue Xiao;Xueliang Zhu
【期刊名称】《细胞研究(英文版)》 【年(卷),期】2012(022)007 【摘要】The
Gβγ
heterodimer
is
an
important
signal
transducer.Gβ,however,is prone to misfolding due to its requirement for Gγ 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 the proteasome.It was sequestered in aggresomes after the inhibition of the proteasome activity with MG132.Sustained activation of Gβγ signaling further elevated cellular levels of the ubiquitinated Gβ.Moreover,Nudel,a regulator of cytoplasmic dynein,the microtubule minus end-directed motor,directly
interacted
with
both
the
unubiquitinated
and
ubiquitinated mfGβ.Increasing the levels of both mfGβ and Nudel promoted the association of Gβ with both Nudel and dynein,resulting in robust aggresome formation in a dynein-dependent manner.Depletion of Nudel by RNAi reduced the dynein-associated mfGβ,impaired the MG132-induced aggresome formation,and markedly prolonged the half-life of nascent Gβ.Therefore,cytosolic mfGβ is recruited to dynein by
Misfolded Gβ is recruited to cytoplasmic dynein by Nudel for efficient clearance
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