Endoplasmic reticulum, membrane protein assembly

Mayer TU, Braun T, Jentsch, S (1998) Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO ] 17 3251-3257 McCracken AA, Brodsky JL (1996) Assembly of ER-associated protein degradation in vitro dependence on cytosol, calnexin, and ATP. J Cell Biol 132 291-298 McDonald HB, Byers B (1997) A proteasome cap subunit required for spindle pole body duplication in yeast. J Cell Biol 137 539-553 McGee TP, Cheng HH, Kumagai H, Omura S, Simoni RD (1996) Degradation of 3-hydroxy-3-methylg utaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J Biol Chem 271 25630-25638... 

Gillece P, Pilon M, Romisch K (2000) The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 97 4609 -4614 Ginsberg HN (1997) Role of lipid synthesis, chaperone proteins and proteasomes in the assembly and secretion of apoprotein B-containing lipoproteins from cultured liver cells. Clin Exp Pharmacol Physiol 24 A29-A32... 

Walter, P., and Blobel, G. (1981b). Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in cdro-assembled polysomes synthesizing secretory protein. J. Cell Biol. 91, 551-556. 

As noted above, synaptic vesicles are not typically generated at the level of the TGN. Instead, they are assembled from endocytosed material retrieved from the synaptic plasma membrane. Synaptic vesicle and plasma membrane lipids and proteins are synthesized in the endoplasmic reticulum and modified in the Golgi apparatus, where they are then packaged in secretory vesicles. These synaptic precursors are delivered to the plasma membrane from the cell body by the constitutive secretory pathway. Synaptic vesicle proteins must be retrieved by clathrin-mediated synaptic vesicle endocytosis, a variant of RME with some neuron-specific components. Once the vesicle sheds its clathrin coat, the uncoated vesicle fuses with a... 

The endoplasmic reticulum (ER) consists of iayered membranes surrounding the nucleus. It is invoived in the transport of chemicais throughout the cytopiasm. Rough endoplasmic reticulum is studded with ribosomes, which are the site of protein assembly from mRNA. Smooth ER lacks ribosomes, and provides channeis for transport of moiecuies... 

Figure 14. Synthesis and assembly of an integral protein into the membrane of the endoplasmic reticulum (based on the data presented in Refs.

Ear less is known about the process of flavivirus assembly. Electron microscopy has shown that immature virions can be found in the lumen of the endoplasmic reticulum (Murphy, 1980). The nucleocapsid core is not assembled free in the cytoplasm rather, its assembly appears to take place on the cytoplasmic face of membranes with which prM and E proteins are associated (Khromykh et al., 2001). The carboxy-terminal signal sequence of the precursor to the capsid protein is thought to anchor that protein to the membrane (Amberg et al., 1994). This should allow interactions to occur between the capsid protein and the envelope proteins, which are also anchored to the membrane but reside in the lumen of the endoplasmic reticulum or vesicles. The capsid protein also contains a conserved stretch of hydrophobic residues located roughly in the middle of the protein that has been suggested to serve as an additional or alternative membrane anchor (Markoff et al., 1997). 

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