Decoding the Interactions of SM Proteins with SNAREs
The success and efficiency of fusion of transport vesicles to target membranes depend upon sets of proteins that are functionally and evolutionarily conserved. The soluble N-ethylmaleimide-sensitive fusion (NSF)-attachment protein receptor (SNARE) family and the Sec1/Munc18 family, also termed SM pr...
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| Format: | Article |
| Language: | English |
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Wiley
2005-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1100/tsw.2005.53 |
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| _version_ | 1850171963918516224 |
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| author | Ren-Wang Peng |
| author_facet | Ren-Wang Peng |
| author_sort | Ren-Wang Peng |
| collection | DOAJ |
| description | The success and efficiency of fusion of transport vesicles to target membranes depend upon sets of proteins that are functionally and evolutionarily conserved. The soluble N-ethylmaleimide-sensitive fusion (NSF)-attachment protein receptor (SNARE) family and the Sec1/Munc18 family, also termed SM proteins, are central players in this process. SM proteins interact with syntaxins of SNARE family, which has been regarded intrinsic for function. By exploring the bi-molecular interactions of SM proteins with syntaxins and their functional implications in vivo in several eukaryotes, which has been enormously facilitated by the availability of the three-dimensional structures of members of both protein families, the long-standing assumption that SM proteins fulfill their regulatory role by binding to syntaxins has to be reconsidered. |
| format | Article |
| id | doaj-art-a6c2a393c9364323bb3b3b3f4fb1472a |
| institution | OA Journals |
| issn | 1537-744X |
| language | English |
| publishDate | 2005-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-a6c2a393c9364323bb3b3b3f4fb1472a2025-08-20T02:20:10ZengWileyThe Scientific World Journal1537-744X2005-01-01547147710.1100/tsw.2005.53Decoding the Interactions of SM Proteins with SNAREsRen-Wang Peng0Max Planck Institute for Biophysical Chemistry, Department of Molecular Genetics, Am Fassberg 11, 37077 Göttingen, GermanyThe success and efficiency of fusion of transport vesicles to target membranes depend upon sets of proteins that are functionally and evolutionarily conserved. The soluble N-ethylmaleimide-sensitive fusion (NSF)-attachment protein receptor (SNARE) family and the Sec1/Munc18 family, also termed SM proteins, are central players in this process. SM proteins interact with syntaxins of SNARE family, which has been regarded intrinsic for function. By exploring the bi-molecular interactions of SM proteins with syntaxins and their functional implications in vivo in several eukaryotes, which has been enormously facilitated by the availability of the three-dimensional structures of members of both protein families, the long-standing assumption that SM proteins fulfill their regulatory role by binding to syntaxins has to be reconsidered.http://dx.doi.org/10.1100/tsw.2005.53 |
| spellingShingle | Ren-Wang Peng Decoding the Interactions of SM Proteins with SNAREs The Scientific World Journal |
| title | Decoding the Interactions of SM Proteins with SNAREs |
| title_full | Decoding the Interactions of SM Proteins with SNAREs |
| title_fullStr | Decoding the Interactions of SM Proteins with SNAREs |
| title_full_unstemmed | Decoding the Interactions of SM Proteins with SNAREs |
| title_short | Decoding the Interactions of SM Proteins with SNAREs |
| title_sort | decoding the interactions of sm proteins with snares |
| url | http://dx.doi.org/10.1100/tsw.2005.53 |
| work_keys_str_mv | AT renwangpeng decodingtheinteractionsofsmproteinswithsnares |