Many neurodegenerative disorders feature the presence of misfolded 
polypeptide-containing intracellular inclusion bodies biochemically and 
morphologically analogous to cellular aggresomes. However, it is largely unknown 
how misfolded polypeptides form aggresomes and are eventually cleared by the 
aggresome-macroautophagy/autophagy pathway, so-called aggrephagy. Our recent 
study revealed that when the ubiquitin-proteasome system is impaired, the 
accumulated misfolded polypeptides are selectively recognized and transported to 
the aggresome by a CED complex. This complex is composed of CTIF, originally 
identified as a specific factor for nuclear cap-binding protein complex (a 
heterodimer of NCBP1/CBP80 and NCBP2/CBP20)-dependent translation (CT), and its 
associated factors EEF1A1 and DCTN1. Aggresomal targeting of a misfolded 
polypeptide via the CED complex is accompanied by CTIF release from the CT 
complex and thereby inhibits CT efficiency. Therefore, our study provides new 
mechanistic insights into the crosstalk between translational inhibition and 
aggresome formation under the influence of a misfolded polypeptide.