Membrane Fusion Intermediates via Directional and Full Assembly of the SNARE Complex.

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Title: Membrane Fusion Intermediates via Directional and Full Assembly of the SNARE Complex.
Authors: Hernandez, Javier M., Stein, Alexander, Behrmann, Elmar, Riedel, Dietmar, Cypionka, Anna, Farsi, Zohreh, Walla, Peter J., Raunser, Stefan, Jahn, Reinhard
Source: Science (pre-March 2025). 6/22/2012, Vol. 336 Issue 6088, p1581-1584. 4p.
Subjects: Cellular control mechanisms, Membrane fusion, SNARE proteins, Bilayer lipid membranes, Intermediates (Chemistry), N-ethylmaleimide sensitive factor, Biochemistry experiments
Abstract: Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Membrane Fusion Intermediates via Directional and Full Assembly of the SNARE Complex.
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  Data: <searchLink fieldCode="AR" term="%22Hernandez%2C+Javier+M%2E%22">Hernandez, Javier M.</searchLink><br /><searchLink fieldCode="AR" term="%22Stein%2C+Alexander%22">Stein, Alexander</searchLink><br /><searchLink fieldCode="AR" term="%22Behrmann%2C+Elmar%22">Behrmann, Elmar</searchLink><br /><searchLink fieldCode="AR" term="%22Riedel%2C+Dietmar%22">Riedel, Dietmar</searchLink><br /><searchLink fieldCode="AR" term="%22Cypionka%2C+Anna%22">Cypionka, Anna</searchLink><br /><searchLink fieldCode="AR" term="%22Farsi%2C+Zohreh%22">Farsi, Zohreh</searchLink><br /><searchLink fieldCode="AR" term="%22Walla%2C+Peter+J%2E%22">Walla, Peter J.</searchLink><br /><searchLink fieldCode="AR" term="%22Raunser%2C+Stefan%22">Raunser, Stefan</searchLink><br /><searchLink fieldCode="AR" term="%22Jahn%2C+Reinhard%22">Jahn, Reinhard</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 6/22/2012, Vol. 336 Issue 6088, p1581-1584. 4p.
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  Data: <searchLink fieldCode="DE" term="%22Cellular+control+mechanisms%22">Cellular control mechanisms</searchLink><br /><searchLink fieldCode="DE" term="%22Membrane+fusion%22">Membrane fusion</searchLink><br /><searchLink fieldCode="DE" term="%22SNARE+proteins%22">SNARE proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Bilayer+lipid+membranes%22">Bilayer lipid membranes</searchLink><br /><searchLink fieldCode="DE" term="%22Intermediates+%28Chemistry%29%22">Intermediates (Chemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22N-ethylmaleimide+sensitive+factor%22">N-ethylmaleimide sensitive factor</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemistry+experiments%22">Biochemistry experiments</searchLink>
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  Data: Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1126/science.1221976
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        Text: English
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      – SubjectFull: Cellular control mechanisms
        Type: general
      – SubjectFull: Membrane fusion
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      – SubjectFull: SNARE proteins
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      – SubjectFull: Bilayer lipid membranes
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      – SubjectFull: Intermediates (Chemistry)
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      – SubjectFull: N-ethylmaleimide sensitive factor
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      – SubjectFull: Biochemistry experiments
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              M: 06
              Text: 6/22/2012
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              Y: 2012
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