NSF and p97/VCP: similar at first, different at last |
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| Authors: | Brunger Axel T DeLaBarre Byron |
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| Institution: | Howard Hughes Medical Institute, and Department of Molecular and Cellular Physiology, and Stanford Synchrotron Radiation Laboratory, Stanford University, James H. Clark Center E300-C, 318 Campus Drive, Stanford, CA 94305-5432, USA. brunger@stanford.edu |
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| Abstract: | N-Ethylmaleimide sensitive factor (NSF) and p97/valosin-containing protein (VCP) are distantly related members of the ATPases associated with a variety of cellular activities (AAA) family of proteins. While both proteins have been implied in cellular morphology changes involving membrane compartments or vesicles, more recent evidence seems to imply that NSF is primarily involved in the soluble NSF attachment receptor (SNARE)-mediated vesicle fusion by disassembling the SNARE complex whereas p97/VCP is primarily involved in the extraction of membrane proteins. These functional differences are now corroborated by major structural differences based on recent crystallographic and cryo-electron microscopy studies. This review discusses these recent findings. |
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| Keywords: | AAA protein Vesicle fusion Membrane protein extraction Endoplasmic reticulum-associated degradation |
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