Phagocytosed Live Listeria monocytogenes Influences Rab5-regulated in Vitro Phagosome-Endosome Fusion

Álvarez-Domínguez, Carmen; Barbieri, Alejandro M.; Berón, Walter; Wandinger‐Ness, Angela; Stahl, Philip D.

doi:10.1074/jbc.271.23.13834

Cited by 141 publications

(134 citation statements)

References 57 publications

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“…Interestingly, high concentrations of NEM (3 mM) cause only a 40% inhibition in this model, suggesting that NSF is protected upon addition of excess EEA1. NEM-resistant fusion events have been described in other in vitro reconstitution assays (36)(37)(38). Our data suggest that activation of Rab promotes not only association of tethering proteins but also of NSF and probably other factors involved in SNARE activation.…”

Section: Discussionsupporting

confidence: 51%

Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N -ethylmaleimide-sensitive factor

Michaut

Tomes²,

Blas³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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The acrosome reaction of spermatozoa is a complex, calciumdependent, regulated exocytosis. Fusion at multiple sites between the outer acrosomal membrane and the cell membrane causes the release of the acrosomal contents and the loss of the membranes surrounding the acrosome. However, very little is known about the molecules that mediate and regulate this unique fusion process. Here, we show that N-ethylmaleimide-sensitive factor (NSF), a protein essential for most fusion events, is present in the acrosome of several mammalian spermatozoa. Moreover, we demonstrate that calcium-dependent exocytosis of permeabilized sperm requires active NSF. Previously, we have shown that the addition of the active (GTP-bound) form of the small GTPase Rab3A triggers exocytosis in permeabilized spermatozoa. In the present report we show that Rab3A is necessary for calcium-dependent exocytosis. The activation of Rab3A protects NSF from N-ethylmaleimide inhibition and precludes the exchange of the endogenous protein with recombinant dominant negative mutants of NSF. Furthermore, Rab3A activation of acrosomal exocytosis requires active NSF. Our results suggest that, upon calcium stimulation, Rab3A switches to its active GTP-bound form, triggering the formation of a protein complex in which NSF is protected. This process is suggested to be an essential part of the molecular mechanism of membrane fusion leading to the release of the acrosomal contents.

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Section: Discussionsupporting

confidence: 51%

Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N -ethylmaleimide-sensitive factor

Michaut

Tomes²,

Blas³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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“…Rab5 is an early endosome marker that associates with phagosomes within the first 10 min of phagocytosis (45,46). Immunostaining of GFP-cPLA 2 ␣-expressing macrophages fixed 5 min after initiation of zymosan phagocytosis revealed a co-localization of Rab5 and GFPcPLA 2 ␣ on nascent phagosomes (Fig.…”

Section: Gfp-cpla 2 ␣ Translocates To the Phagosome During Zymosanmentioning

confidence: 99%

Cytosolic Phospholipase A2 Translocates to Forming Phagosomes during Phagocytosis of Zymosan in Macrophages

Girotti

Evans

Burke

et al. 2004

Journal of Biological Chemistry

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Resident tissue macrophages mediate early innate immune responses to microbial infection. Cytosolic phospholipase A 2 ␣ (cPLA 2 ␣) is activated in macrophages during phagocytosis of non-opsonized yeast (zymosan) triggering arachidonic acid release and eicosanoid production. cPLA 2 ␣ translocates from cytosol to membrane in response to intracellular calcium concentration ([Ca 2؉ ] i ) increases. Enhanced green fluorescent protein (EGFP)-cPLA 2 ␣ translocated to forming phagosomes, surrounding the zymosan particle by 5 min and completely overlapping with early endosome (Rab5) and plasma membrane (F4/80) markers but only partially overlapping with resident endoplasmic reticulum proteins (GRP78 and cyclooxygenase 2). EGFP-cPLA 2 ␣ also localized to membrane ruffles during phagocytosis. Zymosan induced an initial high amplitude calcium transient that preceded particle uptake followed by a low amplitude sustained calcium increase. Both phases were required for optimal phagocytosis. Extracellular calcium chelation prevented only the sustained phase but allowed a limited number of phagocytic events, which were accompanied by translocation of cPLA 2 ␣ to the phagosome although [Ca 2؉ ] i remained at resting levels. The results demonstrate that cPLA 2 ␣ targets the phagosome membrane, which may serve as a source of arachidonic acid for eicosanoid production.

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“…These processes are sometimes targeted by a class of microbes capable of affecting phagosome integrity or maturation (8, 10 -19). Interference with the normal pathway of phagosomal maturation into the phagolysosome enables such intracellular pathogens to avoid microbial growth control or killing by the host phagocytic cells or to avert efficient antigen presentation to the effectors of adaptive immune response in the host (1,3,7,20,21). Consequently, investigations of microbial interference with the trafficking processes in the host cells may provide a means for dissecting the phagosomal maturation pathway.…”

mentioning

confidence: 99%

“…The mechanisms of phagosomal biogenesis and maturation into the phagolysosome represent a fundamental biological process reflecting regulatory aspects of membrane trafficking and organelle biogenesis in eukaryotic cells (1)(2)(3)(4)(5)(6)(7)(8)(9). These processes are sometimes targeted by a class of microbes capable of affecting phagosome integrity or maturation (8, 10 -19).…”

mentioning

confidence: 99%

Cellubrevin Alterations and Mycobacterium tuberculosis Phagosome Maturation Arrest

Fratti¹,

Chua²,

Deretic³

2002

Journal of Biological Chemistry

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The intracellular trafficking processes controlling phagosomal maturation remain to be fully delineated. Mycobacterium tuberculosis var. bovis BCG, an organism that causes phagosomal maturation arrest, has emerged as a tool for dissection of critical phagosome biogenesis events. In this work, we report that cellubrevin, a v-SNARE functioning in endosomal recycling and implicated in endosomal interactions with post-Golgi compartments, plays a role in phagosomal maturation and that it is altered on mycobacterial phagosomes. Both mycobacterial phagosomes, which undergo maturation arrest, and model phagosomes containing latex beads, which follow the normal pathway of maturation into phagolysosomes, acquired cellubrevin. However, the mycobacterial and model phagosomes differed, as a discrete proteolytic degradation of this SNARE was detected on mycobacterial phagosomes. The observed cellubrevin alteration on mycobacterial phagosomes was not a passive event secondary to a maturation arrest at another checkpoint of the phagosome maturation pathway, since pharmacological inhibitors of phagosomal/ endosomal pathways blocking phagosomal maturation did not cause cellubrevin degradation on model phagosomes. Cellubrevin status on phagosomes had consequences on phagosomal membrane and lumenal content trafficking, involving plasma membrane marker recycling and delivery of lysosomal enzymes. These results suggest that cellubrevin plays a role in phagosomal maturation and that it is a target for modification by mycobacteria or by infection-induced processes in the host cell.

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Phagocytosed Live Listeria monocytogenes Influences Rab5-regulated in Vitro Phagosome-Endosome Fusion

Cited by 141 publications

References 57 publications

Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N -ethylmaleimide-sensitive factor

Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N -ethylmaleimide-sensitive factor

Cytosolic Phospholipase A2 Translocates to Forming Phagosomes during Phagocytosis of Zymosan in Macrophages

Cellubrevin Alterations and Mycobacterium tuberculosis Phagosome Maturation Arrest

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