Macroautophagy is a catabolic process by which the cell degrades cytoplasmic 
components through the lysosomal machinery. While initially acknowledged as a 
rather unspecific bulk degradation process, growing lines of evidence indicate 
the selectivity of macroautophagy pathways in the removal of misfolded or 
aggregated proteins. How such substrates are recognized and specifically 
targeted to the macroautophagy machinery has become a hotspot of investigation, 
and recent evidence suggests that here molecular chaperones and co-chaperones 
play a central role. One emerging pathway is mediated by the co-chaperone 
protein Bcl-2-associated athanogene 3 (BAG 3) which seems to utilize the 
specificity of molecular chaperones (heat-shock proteins) towards non-native 
proteins as basis for targeted macroautophagic degradation. In this short 
review, we focus on the molecular interplay between the macroautophagy system 
and molecular chaperones and highlight the relevance of the pathway mediated by 
BAG3 to aging and age-associated protein-misfolding diseases.