All three components of the neuronal SNARE complex contribute to secretory vesicle docking

Wu, Yao; Gu, Yiwen; Morphew, Mary K.; Yao, Jun; Yeh, Felix L.; Dong, Min; Chapman, Edwin R.

doi:10.1083/jcb.201106158

Cited by 21 publications

(14 citation statements)

References 44 publications

(81 reference statements)

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“…, 2000 ), and found an immobile (in x , y ) pool of DCVs directly attached to the plasma membrane that corresponded to ∼65% of the DCVs in our standard TIRF field (Supplemental Figure S1A). This pool of DCVs was strongly reduced by the knockdown of syntaxin-1 and SNAP-25 (Supplemental Figure S1B), consistent with DCVs being in a tethered or docked state ( Wu et al. , 2012 ; Mohrmann et al.…”

Section: Resultssupporting

confidence: 59%

“…Previous studies in chromaffin and PC12 cells documented small pools of DCVs attached via VAMP-2 ( Nofal et al. , 2007 ; Wu et al. , 2012 ).…”

Section: Discussionmentioning

confidence: 94%

“…Many of the ∼100-nm DCVs in the PC12 cell clone used in these studies are attached to the plasma membrane, based on biochemical and morphological studies ( Martin and Kowalchyk, 1997 ; Fujita et al. , 2007 ; Wu et al. , 2012 ).…”

Section: Resultsmentioning

confidence: 99%

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Resident CAPS on dense-core vesicles docks and primes vesicles for fusion

Kabachinski

Kielar-Grevstad

Zhang

et al. 2016

MBoC

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Section: Resultssupporting

confidence: 59%

“…Previous studies in chromaffin and PC12 cells documented small pools of DCVs attached via VAMP-2 ( Nofal et al. , 2007 ; Wu et al. , 2012 ).…”

Section: Discussionmentioning

confidence: 94%

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Resident CAPS on dense-core vesicles docks and primes vesicles for fusion

Kabachinski

Kielar-Grevstad

Zhang

et al. 2016

MBoC

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“…The SNARE complex is central to a mechanism whereby regulatory components of SNARE-mediated membrane fusion regulate the late autolysosomal process in cancer biology [24,52]. Indeed, SNARE proteins are required for autophagy [53,54] and formation of the SNARE complex prompts vesicles to fuse with the plasma membrane [50,55] Our data indicate that the SNAP25mediated autolysosomal process plays an unexpectedly broad role in the biogenesis of autolysosomes as well as their efflux. Because of its prosurvival role under unfavorable conditions, it is not surprising that autophagy protects cancer cells from stresses, such as nutrient deprivation or chemotherapy [56,57].…”

Section: Discussionmentioning

confidence: 78%

NUPR1 maintains autolysosomal efflux by activatingSNAP25transcription in cancer cells

Yan

et al. 2017

Autophagy

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In the advanced stages of cancer, autophagy is thought to promote tumor progression through its ability to mitigate various cellular stresses. However, the details of how autophagy is homeostatically regulated in such tumors are unknown. Here, we report that NUPR1 (nuclear protein 1, transcriptional regulator), a transcriptional coregulator, is aberrantly expressed in a subset of cancer cells and predicts low overall survival rates for lung cancer patients. NUPR1 regulates the late stages of autolysosome processing through the induction of the SNARE protein SNAP25, which forms a complex with the lysosomal SNARE-associated protein VAMP8. NUPR1 depletion deregulates autophagic flux and impairs autolysosomal clearance, inducing massive cytoplasmic vacuolization and premature senescence in vitro and tumor suppression in vivo. Collectively, our data show that NUPR1 is a potent regulator of autolysosomal dynamics and is required for the progression of some epithelial cancers.

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“…SNAP-25 is a critical component of the SNARE complex that controls release of the neurotransmitter acetylcholine. Since acetylcholine is required for neuromuscular and autonomic function (Wu et al, 2012), intoxication by BoNT/A leads to flaccid paralysis and autonomic dysfunction.…”

Section: Introductionmentioning

confidence: 99%

Small molecule metalloprotease inhibitor with in vitro, ex vivo and in vivo efficacy against botulinum neurotoxin serotype A

Jacobson¹,

Adler²,

Silvaggi

et al. 2017

Toxicon

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Botulinum neurotoxins (BoNTs) are the most toxic substances known to mankind and are the causative agents of the neuroparalytic disease botulism. Their ease of production and extreme toxicity have caused these neurotoxins to be classified as Tier 1 bioterrorist threat agents and have led to a sustained effort to develop countermeasures to treat intoxication in case of a bioterrorist attack. While timely administration of an approved antitoxin is effective in reducing the severity of botulism, reversing intoxication requires different strategies. In the present study, we evaluated ABS 252 and other mercaptoacetamide small molecule active-site inhibitors of BoNT/A light chain using an integrated multi-assay approach. ABS 252 showed inhibitory activity in enzymatic, cell-based and muscle activity assays, and importantly, produced a marked delay in time-to-death in mice. The results suggest that a multi-assay approach is an effective strategy for discovery of potential BoNT therapeutic candidates.

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All three components of the neuronal SNARE complex contribute to secretory vesicle docking

Abstract: Docking of large dense-core vesicles is reduced by cleavage of any of the neuronal SNARE complex proteins: synaptobrevin, syntaxin, or SNAP-25.

Cited by 21 publications

References 44 publications

Resident CAPS on dense-core vesicles docks and primes vesicles for fusion

Resident CAPS on dense-core vesicles docks and primes vesicles for fusion

NUPR1 maintains autolysosomal efflux by activatingSNAP25transcription in cancer cells

Small molecule metalloprotease inhibitor with in vitro, ex vivo and in vivo efficacy against botulinum neurotoxin serotype A

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