A critical role for vesicle‐associated membrane protein‐7 in exocytosis from human eosinophils and neutrophils

Logan, Michael; Lacy, Paige; Odemuyiwa, Solomon O.; Steward, Melissa M.; Davoine, Francis; Kita, Hirohito; Moqbel, Redwan

doi:10.1111/j.1398-9995.2006.01089.x

Cited by 86 publications

(92 citation statements)

References 36 publications

(62 reference statements)

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“…We thus propose that VAMP7 mediates regulated exocytosis of LE/Lys in response to neuronal signaling, accounting for recycling of PLP and its inclusion into the myelin domain of the oligodendroglial cell surface. The specific role of VAMP7 in regulated exocytosis of LE/Lys is well established in several cell types (Martinez-Arca et al, 2001;Braun et al, 2004;Rao et al, 2004;Arantes and Andrews, 2006;Logan et al, 2006;ProuxGillardeaux et al, 2007;Marcet-Palacios et al, 2008) and appears primarily associated with cellular processes requiring rapid expansion and remodeling of the plasma membrane (Chaineau et al, 2009;Danglot et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Transport of the Major Myelin Proteolipid Protein Is Directed by VAMP3 and VAMP7

Feldmann¹,

Amphornrat²,

Schönherr³

et al. 2011

J. Neurosci.

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CNS myelination by oligodendrocytes requires directed transport of myelin membrane components and a timely and spatially controlled membrane expansion. In this study, we show the functional involvement of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (R-SNARE) proteins VAMP3/cellubrevin and VAMP7/TI-VAMP in myelin membrane trafficking. VAMP3 and VAMP7 colocalize with the major myelin proteolipid protein (PLP) in recycling endosomes and late endosomes/lysosomes, respectively. Interference with VAMP3 or VAMP7 function using small interfering RNA-mediated silencing and exogenous expression of dominantnegative proteins diminished transport of PLP to the oligodendroglial cell surface. In addition, the association of PLP with myelin-like membranes produced by oligodendrocytes cocultured with cortical neurons was reduced. We furthermore identified Syntaxin-4 and Syntaxin-3 as prime acceptor Q-SNAREs of VAMP3 and VAMP7, respectively. Analysis of VAMP3-deficient mice revealed no myelination defects. Interestingly, AP-3␦-deficient mocha mice, which suffer from impaired secretion of lysosome-related organelles and missorting of VAMP7, exhibit a mild dysmyelination characterized by reduced levels of select myelin proteins, including PLP. We conclude that PLP reaches the cell surface via at least two trafficking pathways with distinct regulations: (1) VAMP3 mediates fusion of recycling endosomederived vesicles with the oligodendroglial plasma membrane in the course of the secretory pathway; (2) VAMP7 controls exocytosis of PLP from late endosomal/lysosomal organelles as part of a transcytosis pathway. Our in vivo data suggest that exocytosis of lysosomerelated organelles controlled by VAMP7 contributes to myelin biogenesis by delivering cargo to the myelin membrane.

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Section: Discussionmentioning

confidence: 99%

Transport of the Major Myelin Proteolipid Protein Is Directed by VAMP3 and VAMP7

Feldmann¹,

Amphornrat²,

Schönherr³

et al. 2011

J. Neurosci.

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“…In a variety of secretory cells, the formation of SNARE complexes is a major event preceding membrane fusion and mediator release (13,14). A range of SNARE proteins has been identified in neutrophils, and there is much evidence that indicates their implication in the regulation of granule fusion (13,(15)(16)(17)(18)(19). Munc13 proteins constitute a family of four mammalian homologs of Caenorhabditis elegans Unc-13.…”

Section: Munc13-4 Regulates Granule Secretion In Human Neutrophilsmentioning

confidence: 99%

“…In particular, it may regulate the interactions between soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptors (SNAREs) located on granules/vesicles (v-SNAREs) and the plasma membrane (t-SNAREs) (1,2,12). In a variety of secretory cells, the formation of SNARE complexes is a major event preceding membrane fusion and mediator release (13,14). A range of SNARE proteins has been identified in neutrophils, and there is much evidence that indicates their implication in the regulation of granule fusion (13,(15)(16)(17)(18)(19).…”

Section: Munc13-4 Regulates Granule Secretion In Human Neutrophilsmentioning

confidence: 99%

Munc13-4 Regulates Granule Secretion in Human Neutrophils

Pivôt-Pajot

Varoqueaux

Basile

et al. 2008

The Journal of Immunology

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The neutrophil plays a central role in the innate host immune defense. Regulated exocytosis of its granules and release of antimicrobial and cytotoxic substances are key events to limit the spread of pathogens. However, the molecular mechanisms that control exocytosis of neutrophil granules are ill-defined. Recently, it was shown that Munc13-4 is essential for the priming of granules in several hematopoietic cells. In this study, we show that Munc13-4 is expressed in human neutrophils, and that its expression is increased during granulocytic differentiation of HL-60 and PLB-985 cells. Cell fractionation analysis reveals that Munc13-4 is mainly cytosolic and is recruited rapidly to membranes following stimulation with fMLF (N-formyl-methionyl-leucyl-phenylalanine). Moreover, a pool of Munc13-4 associated with mobilizable secondary and tertiary granules is relocalized to the plasma membrane after stimulation with fMLF. The fMLF-induced translocation of Munc13-4 is strictly dependent on calcium in neutrophils. C2 domains of Munc13-4 are essential for binding to phospholipid vesicles in a Ca2+-independent manner. Finally, down-regulation of Munc13-4 using small interfering RNA decreases exocytosis of tertiary granules in PLB-985 cells, whereas overexpression of Munc13-4 enhances secretion of MMP-9 (matrix metalloproteinase-9) from tertiary granules. Our findings suggest a role for Munc13-4 as a component of the secretory machinery in neutrophils.

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“…TI-VAMP labels a compartment of late endosomal/lysosomal origin TI-VAMP has been shown to be involved in fusion processes along the endocytic pathways (Advani et al, 1999;Pryor et al, 2004) and has been indicated as the v-SNARE which mediates secretion of granules of lysosomal nature in several cell types (Casey et al, 2007;Logan et al, 2006;Oishi et al, 2006;Proux-Gillardeaux et al, 2007;Rao et al, 2004;Sander et al, 2008). TI-VAMP fused to GFP was over-expressed by transfection and astrocytes were stained for the early endosome marker EAA1 and for the late endosome-lysosome markers CD63.…”

Section: Ti-vamp Vesicles Represent An Exocytic Pathway Distinct Frommentioning

confidence: 99%

TI‐VAMP/VAMP7 is the SNARE of secretory lysosomes contributing to ATP secretion from astrocytes

Verderio

Cagnoli

Bergami

et al. 2012

Biology of the Cell

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Background information. ATP is the main transmitter stored and released from astrocytes under physiological and pathological conditions. Morphological and functional evidence suggest that besides secretory granules, secretory lysosomes release ATP. However, the molecular mechanisms involved in astrocytic lysosome fusion remain still unknown.Results. In the present study, we identify tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP, also called VAMP7) as the vesicular SNARE which mediates secretory lysosome exocytosis, contributing to release of both ATP and cathepsin B from glial cells. We also demonstrate that fusion of secretory lysosomes is triggered by slow and locally restricted calcium elevations, distinct from calcium spikes which induce the fusion of glutamate-containing clear vesicles. Downregulation of TI-VAMP/VAMP7 expression inhibited the fusion of ATPstoring vesicles and ATP-mediated calcium wave propagation. TI-VAMP/VAMP7 downregulation also significantly reduced secretion of cathepsin B from glioma.Conclusions. Given that sustained ATP release from glia upon injury greatly contributes to secondary brain damage and cathepsin B plays a critical role in glioma dissemination, TI-VAMP silencing can represent a novel strategy to control lysosome fusion in pathological conditions.

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A critical role for vesicle‐associated membrane protein‐7 in exocytosis from human eosinophils and neutrophils

Abstract: Our observations indicate for the first time a critical role for VAMP-7 in both eosinophil and neutrophil mediator release.

Cited by 86 publications

References 36 publications

Transport of the Major Myelin Proteolipid Protein Is Directed by VAMP3 and VAMP7

Transport of the Major Myelin Proteolipid Protein Is Directed by VAMP3 and VAMP7

Munc13-4 Regulates Granule Secretion in Human Neutrophils

TI‐VAMP/VAMP7 is the SNARE of secretory lysosomes contributing to ATP secretion from astrocytes

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