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Quality Control of Transmembrane Proteins
Wednesday, March 23, 2005,
3:00:00 PM Time displayed is Eastern Time, Washington DC Local
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Cells maintain their integrity by constantly seeking out and degrading damaged or misfolded proteins. For proteins in solution, it is the exposure of hydrophobic amino acids that normally are buried in the interior that signifies misfolding, and it is these that are recognised by molecular chaperones. For the lipid-embedded portions of transmembrane proteins, the converse holds – exposure of hydrophilic residues to the lipid bilayer can cause aggregation and is often sufficient to promote rapid degradation. Thus, for example, incompletely assembled forms of the T cell receptor (which is held together by polar interactions within the bilayer) are either held in the Endoplasmic Reticulum and degraded there, or transported to lysosomes for disposal.