The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex
Soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins constitute the core of an ancient vesicle fusion machine that diversified into distinct sets that now function in different trafficking steps in eukaryotic cells. Deciphering their precise mod...
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| Format: | Article |
| Language: | en_US |
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National Academy of Sciences (U.S.)
2015
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| Online Access: | http://hdl.handle.net/1721.1/96338 https://orcid.org/0000-0002-3866-2742 |
| _version_ | 1826191622297092096 |
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| author | Demircioglu, Fatma Esra Fasshauer, Dirk Burkhardt, Pawel |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Demircioglu, Fatma Esra Fasshauer, Dirk Burkhardt, Pawel |
| author_sort | Demircioglu, Fatma Esra |
| collection | MIT |
| description | Soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins constitute the core of an ancient vesicle fusion machine that diversified into distinct sets that now function in different trafficking steps in eukaryotic cells. Deciphering their precise mode of action has proved challenging. SM proteins are thought to act primarily through one type of SNARE protein, the syntaxins. Despite high structural similarity, however, contrasting binding modes have been found for different SM proteins and syntaxins. Whereas the secretory SM protein Munc18 binds to the ‟closed conformation” of syntaxin 1, the ER–Golgi SM protein Sly1 interacts only with the N-peptide of Sed5. Recent findings, however, indicate that SM proteins might interact simultaneously with both syntaxin regions. In search for a common mechanism, we now reinvestigated the Sly1/Sed5 interaction. We found that individual Sed5 adopts a tight closed conformation. Sly1 binds to both the closed conformation and the N-peptide of Sed5, suggesting that this is the original binding mode of SM proteins and syntaxins. In contrast to Munc18, however, Sly1 facilitates SNARE complex formation by loosening the closed conformation of Sed5. |
| first_indexed | 2024-09-23T08:58:46Z |
| format | Article |
| id | mit-1721.1/96338 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T08:58:46Z |
| publishDate | 2015 |
| publisher | National Academy of Sciences (U.S.) |
| record_format | dspace |
| spelling | mit-1721.1/963382022-09-30T12:34:38Z The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex Demircioglu, Fatma Esra Fasshauer, Dirk Burkhardt, Pawel Massachusetts Institute of Technology. Department of Biology Demircioglu, Fatma Esra Soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins constitute the core of an ancient vesicle fusion machine that diversified into distinct sets that now function in different trafficking steps in eukaryotic cells. Deciphering their precise mode of action has proved challenging. SM proteins are thought to act primarily through one type of SNARE protein, the syntaxins. Despite high structural similarity, however, contrasting binding modes have been found for different SM proteins and syntaxins. Whereas the secretory SM protein Munc18 binds to the ‟closed conformation” of syntaxin 1, the ER–Golgi SM protein Sly1 interacts only with the N-peptide of Sed5. Recent findings, however, indicate that SM proteins might interact simultaneously with both syntaxin regions. In search for a common mechanism, we now reinvestigated the Sly1/Sed5 interaction. We found that individual Sed5 adopts a tight closed conformation. Sly1 binds to both the closed conformation and the N-peptide of Sed5, suggesting that this is the original binding mode of SM proteins and syntaxins. In contrast to Munc18, however, Sly1 facilitates SNARE complex formation by loosening the closed conformation of Sed5. Universität Göttingen. Graduate School for Neurosciences and Molecular Biosciences (Fellowship) 2015-04-02T17:14:42Z 2015-04-02T17:14:42Z 2014-09 2014-05 Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/96338 Demircioglu, F. E., P. Burkhardt, and D. Fasshauer. “The SM Protein Sly1 Accelerates Assembly of the ER-Golgi SNARE Complex.” Proceedings of the National Academy of Sciences 111, no. 38 (September 4, 2014): 13828–13833. https://orcid.org/0000-0002-3866-2742 en_US http://dx.doi.org/10.1073/pnas.1408254111 Proceedings of the National Academy of Sciences of the United States of America Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences (U.S.) National Academy of Sciences (U.S.) |
| spellingShingle | Demircioglu, Fatma Esra Fasshauer, Dirk Burkhardt, Pawel The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex |
| title | The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex |
| title_full | The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex |
| title_fullStr | The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex |
| title_full_unstemmed | The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex |
| title_short | The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex |
| title_sort | sm protein sly1 accelerates assembly of the er golgi snare complex |
| url | http://hdl.handle.net/1721.1/96338 https://orcid.org/0000-0002-3866-2742 |
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