The synaptic SNARE complex is a parallel four-stranded helical bundle

Poirier, Michelle A.; Xiao, Wenzhong; Macosko, Jed C.; Chan, Charles; Shin, Yeon‐Kyun; Bennett, Mark K.

doi:10.1038/1799

Cited by 471 publications

(393 citation statements)

References 30 publications

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“…In the past several years, spin-labeling EPR has proven to be a very useful technique in the study of protein structure and function+ In 1998, the structure of the neuronal SNARE complex was determined based on EPR distance and was a powerful demonstration of the ability of EPR to be a structural technique (Poirier et al+, 1998)+ In systems where other techniques have difficulty, such as with membrane proteins, EPR has proven itself to be extremely valuable (Altenbach et al+, 1994;Macosko et al+, 1997)+ Furthermore, the ability of EPR to resolve dynamic changes in proteins, sometimes in a time-resolved fashion, has been exploited to study the function of several important proteins+…”

Section: Resultsmentioning

confidence: 99%

A novel 5′ displacement spin-labeling technique for electron paramagnetic resonance spectroscopy of RNA

Macosko

Pio²,

Tinoco³

et al. 1999

RNA

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An RNA spin-labeling technique was developed using the well-characterized interaction between the HIV Rev peptide and the Rev response element (RRE) RNA as a model system. Spin-labeled RNA molecules were prepared by incorporating guanosine monophosphorothioate (GMPS) at the 59 end using T7 RNA polymerase and then covalently attaching a thiol-specific nitroxide spin label. Three different constructs of the RRE RNA were made by strategically displacing the 59 end within the native three-dimensional structure. Nitroxide-to-nitroxide distance measurements were made between the specifically bound RNA and peptide using electron paramagnetic resonance (EPR) spectroscopy. The dipolar EPR method can reliably measure distances up to 25 Å, the calculation of which is derived from the 1/r 3 dependence of the broadening of EPR lines in motionally frozen samples. This RNA-labeling technique, dubbed 59 displacement spin labeling, extends the usefulness of the dipolar EPR method developed for analysis of protein structure. The advantage of this technique is that it is applicable to large RNA systems such as the ribosome, which are difficult to study by other structural methods.

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Section: Resultsmentioning

confidence: 99%

A novel 5′ displacement spin-labeling technique for electron paramagnetic resonance spectroscopy of RNA

Macosko

Pio²,

Tinoco³

et al. 1999

RNA

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“…One class of membrane-trafficking proteins, referred to as soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), proteins of the vesicle-associated membrane protein (VAMP) and syntaxin families, have been implicated in mediating membrane fusion through their compartment-specific localizations and protein interactions Bock and Scheller, 1999;Pfeffer, 1999). Formation of a very stable four-stranded helical bundle, composed of SNAREs from opposing membranes, is thought to be the biochemical event that drives membrane fusion (Hanson et al, 1997;Lin and Scheller, 1997;Poirier et al, 1998;Sutton et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

Steegmaier

Oorschot

Klumperman

et al. 2000

MBoC

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The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular ER membranes that are abundant in steroidogenic cells.

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“…The products of three of these genes, VAMP (also called synaptobrevin), SNAP-25, and syntaxin, are collectively referred to as SNAREs (Südhof, 1995). These proteins form a core fusion complex that is composed of a four-helical bundle spanning the vesicle and target membranes (Poirier et al, 1998a;Sutton et al, 1998). Formation of this complex is a late step in the membrane fusion process and perhaps actually drives fusion of the lipid bilayers (Hanson et al, 1997;Lin and Scheller, 1997).…”

mentioning

confidence: 99%

Phosphorylated Syntaxin 1 Is Localized to Discrete Domains Along a Subset of Axons

et al. 2000

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Syntaxin 1 is a SNARE protein that plays a central role in synaptic vesicle (SV) exocytosis. We generated an antibody that specifically recognizes a casein kinase II-mediated phosphorylation on serine-14 of syntaxin 1. In this report we show that this phosphorylation occurs in vivo and is developmentally regulated in the rat brain, rising to a level of 40% of the total syntaxin in adult animals. Phosphorylated syntaxin is preferentially associated with SNAP-25 and localizes to discrete domains of the axonal plasma membrane that do not colocalize with pools of synaptic vesicles. These phosphosyntaxin domains may define fusion sites for a novel class of vesicles outside classical active zones.

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The synaptic SNARE complex is a parallel four-stranded helical bundle

Cited by 471 publications

References 30 publications

A novel 5′ displacement spin-labeling technique for electron paramagnetic resonance spectroscopy of RNA

A novel 5′ displacement spin-labeling technique for electron paramagnetic resonance spectroscopy of RNA

Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

Phosphorylated Syntaxin 1 Is Localized to Discrete Domains Along a Subset of Axons

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