Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane protein 7) form an active SNARE complex for early macropinocytic compartment fusion in Dictyostelium discoideum

Bogdanovic, Aleksandra; Bennett, Nelly; Kieffer, Sylvie; Louwagie, Mathilde; Morio, Takahiro; Garin, Jérôme; Satre, Michel; Brückert, Franz

doi:10.1042/bj20020845

Cited by 47 publications

(37 citation statements)

References 49 publications

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“…Localization and structure of the Golgi apparatus in embryonic neuroepithelial cells and adult neurons was normal as examined by electron microscopy or by GM130 immunostaining (data not shown). In contrast, the localization of Vamp7 (also known as TI-VAMP), a vesicle SNARE involved in apical membrane transport in epithelial cells 22,23 and neurons 24,25 , was strongly apical in normal neuroepithelial cells and profoundly disrupted in hyh mutants (Fig. 5k,l), suggesting that partial loss of αSnap disrupted its apical targeting function without disrupting all its cellular functions.…”

Section: Nature Genetics Volume 36 | Number 3 | March 2004 267mentioning

confidence: 97%

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

et al. 2004

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The hyh (hydrocephalus with hop gait) mouse shows a markedly small cerebral cortex at birth and dies postnatally from progressive enlargement of the ventricular system 1,2 . Here we show that the small hyh cortex reflects altered cell fate. Neural progenitor cells withdraw prematurely from the cell cycle, producing more early-born, deep-layer cerebral cortical neurons but depleting the cortical progenitor pool, such that late-born, upper-layer cortical neurons are underproduced, creating a small cortex. hyh mice carry a hypomorphic missense mutation in the gene Napa encoding soluble N-ethylmaleimidesensitive factor (NSF) attachment protein alpha (αSnap), involved in SNAP receptor (SNARE)-mediated vesicle fusion in many cellular contexts. A targeted null Napa mutation is embryonically lethal. Altered neural cell fate is accompanied by abnormal localization of many apical proteins implicated in regulation of neural cell fate, including E-cadherin, β-catenin, atypical protein kinase C (aPKC) and INADL (inactivation-noafterpotential D-like, also known as protein associated with Lin7, or Pals1). Apical localization of the SNARE Vamp7 is also disrupted. Thus, αSnap is essential for apical protein localization and cell fate determination in neuroepithelial cells.

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Section: Nature Genetics Volume 36 | Number 3 | March 2004 267mentioning

confidence: 97%

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

et al. 2004

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“…There is some supporting evidence in yeast that Use1p/Slt1p interacts with Ykt6p (8), which participates in the membrane fusion of vacuoles. Similarly, we observed an interaction between D12 and VAMP7, which is involved in phagocytosis or trafficking between endosomes and lysosomes (55)(56)(57). Interestingly, we observed that the 17.2-kDa fragment of D12 failed to bind to VAMP7, although it did bind syntaxin 18 and Sec22b, and fragments longer than 17.8 kDa bound to VAMP7 (Fig.…”

Section: Discussionmentioning

confidence: 71%

Involvement of a Novel Q-SNARE, D12, in Quality Control of the Endomembrane System

Okumura

Hatsuzawa

Tamura

et al. 2006

Journal of Biological Chemistry

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The cellular endomembrane system requires the proper kinetic balance of synthesis and degradation of its individual components, which is maintained in part by a specific membrane fusion apparatus. In this study, we describe the molecular properties of D12, which was identified from a mouse expression library. This C-terminal anchored membrane protein has sequence similarity to both a yeast soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE), Use1p/Slt1p, and a recently identified human syntaxin 18-binding protein, p31. D12 formed a tight complex with syntaxin 18 as well as Sec22b and bound to ␣-SNAP, indicating that D12 is a SNARE protein. Although the majority of D12 is located in the endoplasmic reticulum and endoplasmic reticulum-Golgi intermediate compartments at steady state, overexpression or knockdown of D12 had no obvious effects on membrane trafficking in the early secretory pathway. However, suppression of D12 expression caused rapid appearance of lipofuscin granules, accompanied by apoptotic cell death without the apparent activation of the unfolded protein response. The typical cause of lipofuscin formation is the impaired degradation of mitochondria by lysosomal degradative enzymes, and, consistent with this, we found that proper post-Golgi maturation of cathepsin D was impaired in D12-deficient cells. This unexpected observation was supported by evidence that D12 associates with VAMP7, a SNARE in the endosomallysosomal pathway. Hence, we suggest that D12 participates in the degradative function of lysosomes.

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“…It is possible that the fusion events also involved one of the hits in our RNAi screen, vesicle‐associated membrane protein 7 (VAMP7). It has been shown to mediate pinosome fusion events in Dictyostelium discoideum 58.…”

Section: Discussionmentioning

confidence: 99%

Vaccinia Virus Infection Requires Maturation of Macropinosomes

Rizopoulos

Balistreri

Kilcher

et al. 2015

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The prototypic poxvirus, vaccinia virus (VACV), occurs in two infectious forms, mature virions (MVs) and extracellular virions (EVs). Both enter HeLa cells by inducing macropinocytic uptake. Using confocal microscopy, live‐cell imaging, targeted RNAi screening and perturbants of endosome maturation, we analyzed the properties and maturation pathway of the macropinocytic vacuoles containing VACV MVs in HeLa cells. The vacuoles first acquired markers of early endosomes [Rab5, early endosome antigen 1 and phosphatidylinositol(3)P]. Prior to release of virus cores into the cytoplasm, they contained markers of late endosomes and lysosomes (Rab7a, lysosome‐associated membrane protein 1 and sorting nexin 3). RNAi screening of endocytic cell factors emphasized the importance of late compartments for VACV infection. Follow‐up perturbation analysis showed that infection required Rab7a and PIKfyve, confirming that VACV is a late‐penetrating virus dependent on macropinosome maturation. VACV EV infection was inhibited by depletion of many of the same factors, indicating that both infectious particle forms share the need for late vacuolar conditions for penetration.

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Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane protein 7) form an active SNARE complex for early macropinocytic compartment fusion in Dictyostelium discoideum

Abstract: The macropinocytic pathway in Dictyostelium discoideum is organized linearly. After actin-driven internalization, fluid material passes sequentially from endosomes to lysosomes, where molecules are degraded and absorbed.

Cited by 47 publications

References 49 publications

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

Involvement of a Novel Q-SNARE, D12, in Quality Control of the Endomembrane System

Vaccinia Virus Infection Requires Maturation of Macropinosomes

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