The 20S proteasome assembly is an ATP-dependent process, and the increased presence of mitochondrial proteins suggests that upon Thiocolchicoside D-maltose and D-xylose LW479 induction a larger fraction of the mitochondria are associated with the ER, thereby facilitating the export of ATP and consequently the 20S proteasome assembly. As for the remainder of the proteins, several cargo proteins were specific for one or both inducing conditions. Glucoamylase A was found more abundant on D-maltose, b-xylosidase XlnD was only detected on D-xylose, and acid a-amylase AamA was found on both conditions, though more abundant on D-maltose compared to D-xylose. D-Maltose induction also increased endosomal-cargo receptor Erv14, histone H4 and the protein component of the large subunit Rpl15. Several proteins were found to be induced by D-maltose or D-xylose, however, only a few proteins were found in decreased amounts under these conditions. The main microsomal proteins that were repressed upon the D-maltose and D-xylose conditions were the cytoplasmic chaperone CypA, the phosphatidylinositolphosphatidylcholine transfer Sec14 protein and the three metabolic enzymes glycerol dehydrogenase, 3-phosphoglycerate dehydrogenase and ornithine carbamoyl-transferase. In addition, an unknown protein from the perilipin family was decreased on D-maltose. The comparative analysis of the secretome and the microsomal proteome reveals that the 29 cargo proteins are both present in the secretory organelles as well as secreted outside of the cell, whereas the anchored secreted proteins are predominantly found in the microsomal fractions. Although the secreted proteins GlaA, AamA, AgdA, XlnD, LacA and BglA etc are equally abundant in the microsomal and thesecreted fractions, the anchored proteins do not appear in both fractions equally. Also the comparison of protein relative amounts present in the secretome and in microsomes is also difficult because of the factor time, since due to the experimental set up, the secreted proteins accumulated over a period of 16 h. The microsomal proteome on the other hand was the result of microsomes isolated in a defined moment in time; therefore some proteins might accumulate whereas others might be immediately secreted.