RGD Reference Report - Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover. - Rat Genome Database

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Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.

Authors: Ryu, Je-Kyung  Min, Duyoung  Rah, Sang-Hyun  Kim, Soo Jin  Park, Yongsoo  Kim, Haesoo  Hyeon, Changbong  Kim, Ho Min  Jahn, Reinhard  Yoon, Tae-Young 
Citation: Ryu JK, etal., Science. 2015 Mar 27;347(6229):1485-9. doi: 10.1126/science.aaa5267.
RGD ID: 13432338
Pubmed: PMID:25814585   (View Abstract at PubMed)
PMCID: PMC4441202   (View Article at PubMed Central)
DOI: DOI:10.1126/science.aaa5267   (Journal Full-text)

During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (α-SNAP) disassemble the soluble NSF attachment protein receptor (SNARE) complex for recycling of the SNARE proteins. The molecular mechanism by which NSF disassembles the SNARE complex is largely unknown. Using single-molecule fluorescence spectroscopy and magnetic tweezers, we found that NSF disassembled a single SNARE complex in only one round of adenosine triphosphate (ATP) turnover. Upon ATP cleavage, the NSF hexamer developed internal tension with dissociation of phosphate ions. After latent time measuring tens of seconds, NSF released the built-up tension in a burst within 20 milliseconds, resulting in disassembly followed by immediate release of the SNARE proteins. Thus, NSF appears to use a "spring-loaded" mechanism to couple ATP hydrolysis and unfolding of substrate proteins.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein binding enablesIPIUniProtKB:P6304513432338PMID:25814585IntAct 
protein binding enablesIPIUniProtKB:P60881-213432338PMID:25814585IntAct 

Objects Annotated

Genes (Rattus norvegicus)
Snap25  (synaptosome associated protein 25)
Vamp2  (vesicle-associated membrane protein 2)


Additional Information