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Vol. 12, Issue 6, 1711-1723, June 2001
Department of Cell Research and Immunology, George Wise Faculty of
Life Sciences, Tel Aviv University, Tel Aviv, Israel, 69978
Degradation of proteins that, because of improper or suboptimal
processing, are retained in the endoplasmic reticulum (ER) involves
retrotranslocation to reach the cytosolic ubiquitin-proteasome machinery. We found that substrates of this pathway, the precursor of
human asialoglycoprotein receptor H2a and free heavy chains of murine
class I major histocompatibility complex (MHC), accumulate in a novel
preGolgi compartment that is adjacent to but not overlapping with the
centrosome, the Golgi complex, and the ER-to-Golgi intermediate compartment (ERGIC). On its way to degradation, H2a associated increasingly after synthesis with the ER translocon Sec61.
Nevertheless, it remained in the secretory pathway upon proteasomal
inhibition, suggesting that its retrotranslocation must be tightly
coupled to the degradation process. In the presence of proteasomal
inhibitors, the ER chaperones calreticulin and calnexin, but not BiP,
PDI, or glycoprotein glucosyltransferase, concentrate in the
subcellular region of the novel compartment. The "quality control"
compartment is possibly a subcompartment of the ER. It depends on
microtubules but is insensitive to brefeldin A. We discuss the
possibility that it is also the site for concentration and
retrotranslocation of proteins that, like the mutant cystic fibrosis
transmembrane conductance regulator, are transported to the cytosol,
where they form large aggregates, the "aggresomes."
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