[HTML][HTML] Apolipoprotein B100 exit from the endoplasmic reticulum (ER) is COPII-dependent, and its lipidation to very low density lipoprotein occurs post-ER
V Gusarova, JL Brodsky, EA Fisher - Journal of Biological Chemistry, 2003 - ASBMB
Hepatic apolipoprotein B100 (apoB100) associates with lipids to form dense lipoprotein
particles in the endoplasmic reticulum (ER) and is further lipidated to very low density
lipoproteins (VLDL). Because the VLDL diameter can exceed 200 nm, classical ER-derived
vesicles may be unable to accommodate VLDLs. Using hepatic membranes and cytosol to
reconstitute ER budding, apoB100-containing vesicles sedimented distinct from those
harboring more typical cargo but contained Sec23. Moreover, ER exit of apoB was inhibited …
particles in the endoplasmic reticulum (ER) and is further lipidated to very low density
lipoproteins (VLDL). Because the VLDL diameter can exceed 200 nm, classical ER-derived
vesicles may be unable to accommodate VLDLs. Using hepatic membranes and cytosol to
reconstitute ER budding, apoB100-containing vesicles sedimented distinct from those
harboring more typical cargo but contained Sec23. Moreover, ER exit of apoB was inhibited …
