Folding and assembly of viral membrane proteins

Virology
R W DomsA Helenius

Abstract

It is now clear that folding in the ER is a dynamic, energy-driven process involving a host of cellular folding enzymes and molecular chaperones (see Fig. 1). Within this high-capacity folding environment, nascent molecules fold quickly and efficiently, while misfolded proteins are recognized and retained, being either degraded or rescued. The quality control mechanisms which account for this selective retention are most likely redundant and general in nature--an almost innumerable number of structures, from both endogenous and exogenous proteins, are operated on with equal efficiency. Studies with viral membrane proteins will continue to help illuminate these processes and have contributed greatly to the concepts of conformational maturation and quality control. Furthermore, while the effects of mutations on protein structure and transport cannot always be predicted, useful generalizations can now be made to help develop experimental strategies. Future studies will have to address a variety of unresolved issues. Given the almost limitless sequence and structural variability exhibited by proteins which fold in the ER, no one molecular chaperone is likely to be able to bind to all folding intermediates. Thus, GRP78-BiP is likely...Continue Reading

Citations

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