A multisubunit particle implicated in membrane fusion Journal Article
| Authors: | Wilson, D. W.; Whiteheart, S. W.; Wiedmann, M.; Brunner, M.; Rothman, J. E. |
| Article Title: | A multisubunit particle implicated in membrane fusion |
| Abstract: | The N-ethylmaleimide sensitive fusion protein (NSF) is required for fusion of lipid bilayers at many locations within eukaryotic cells. Binding of NSF to Golgi membranes is known to require an integral membrane receptor and one or more members of a family of related soluble NSF attachment proteins (α-, β-, and γ-SNAPs). Here we demonstrate the direct interaction of NSF, SNAPs and an integral membrane component in a detergent solubilized system. We show that NSF only binds to SNAPs in the presence of the integral receptor, resulting in the formation of a multisubunit protein complex with a sedimentation coefficient of 20S. Particle assembly reveals striking differences between members of the SNAP protein family; γ-SNAP associates with the complex via a binding site distinct from that used by α- and β- SNAPs, which are themselves equivalent, alternative subunits of the particle. Once formed, the 20S particle is subsequently able to disassemble in a process coupled to the hydrolysis of ATP. We suggest how cycles of complex assembly and disassembly could help confer specificity to the generalized NSF-dependent fusion apparatus. |
| Keywords: | nonhuman; animal; animal tissue; complex formation; models, biological; protein assembly; protein protein interaction; animalia; liver; eukaryota; carrier proteins; membrane protein; rat; rats; adenosine triphosphate; hydrolysis; receptors, cell surface; solubility; golgi complex; detergent; membrane fusion; membrane receptor; golgi apparatus; priority journal; article; sedimentation rate; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; n ethylmaleimide; macromolecular systems |
| Journal Title: | Journal of Cell Biology |
| Volume: | 117 |
| Issue: | 3 |
| ISSN: | 0021-9525 |
| Publisher: | Rockefeller University Press |
| Date Published: | 1992-05-01 |
| Start Page: | 531 |
| End Page: | 538 |
| Language: | English |
| DOI: | 10.1083/jcb.117.3.531 |
| PUBMED: | 1315316 |
| PROVIDER: | scopus |
| PMCID: | PMC2289450 |
| DOI/URL: | |
| Notes: | Article -- Source: Scopus |
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