Syntaxin 7 mediates endocytic trafficking to late endosomes

Nakamura, Norihiro; Yamamoto, Akinaru; Wada, Yoh; Futai, Masamitsu

doi:10.1042/bst028a353a

Cited by 37 publications

(44 citation statements)

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“…Finally, we think that the identification of Syntaxin 7 as a lysosomal SNARE is consistent with the strong biochemical and genetic data demonstrating that the yeast homologue Vam3p is a vacuolar SNARE involved in both vacuolar traffic and homotypic fusion (Becherer et al, 1996;Darsow et al, 1997;Peterson et al, 1999;Ungermann et al, 1999). Nakamura et al (2000) demonstrated that expression of Syntaxin 7 in yeast complemented vam3 and pep12 mutants. This observation reinforces the idea that Syntaxin 7 functions in late endocytic compartments.…”

Section: Discussionsupporting

confidence: 49%

“…Prekeris et al (1999) colocalized Syntaxin 7 and anti-transferrin receptor antibodies by both fluorescence and electron microscopy with the use of several different cell types. More recently, Nakamura et al (2000), again with the use of fluorescence and electron microscopy, localized Syntaxin 7 in NIH 3T3 and NRK cells to Lamp 2-positive compartments, suggesting a late endosomal/lysosomal location. Our studies used freshly obtained alveolar macrophages, whereas the other studies used cultured cell types.…”

Section: Discussionmentioning

confidence: 99%

“…Two groups suggested that Syntaxin 7 was associated with early endosomes (Wong et al, 1998;Prekeris et al, 1999), whereas a third group suggested that Syntaxin 7 was localized to late endocytic compartments (Nakamura et al, 2000). Each study used different cell types and different methods for organelle identification.…”

Section: Discussionmentioning

confidence: 99%

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Syntaxin 7 and VAMP-7 are SolubleN-Ethylmaleimide–sensitive Factor Attachment Protein Receptors Required for Late Endosome–Lysosome and Homotypic Lysosome Fusion in Alveolar Macrophages

Ward

Pevsner

Scullion

et al. 2000

MBoC

128

116

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Endocytosis in alveolar macrophages can be reversibly inhibited, permitting the isolation of endocytic vesicles at defined stages of maturation. Using an in vitro fusion assay, we determined that each isolated endosome population was capable of homotypic fusion. All vesicle populations were also capable of heterotypic fusion in a temporally specific manner; early endosomes, isolated 4 min after internalization, could fuse with endosomes isolated 8 min after internalization but not with 12-min endosomes or lysosomes. Lysosomes fuse with 12-min endosomes but not with earlier endosomes. Using homogenous populations of endosomes, we have identified Syntaxin 7 as a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) required for late endosome–lysosome and homotypic lysosome fusion in vitro. A bacterially expressed human Syntaxin 7 lacking the transmembrane domain inhibited homotypic late endosome and lysosome fusion as well as heterotypic late endosome–lysosome fusion. Affinity-purified antibodies directed against Syntaxin 7 also inhibited lysosome fusion in vitro but had no affect on homotypic early endosome fusion. Previous work suggested that human VAMP-7 (vesicle-associated membrane protein-7) was a SNARE required for late endosome–lysosome fusion. A bacterially expressed human VAMP-7 lacking the transmembrane domain inhibited both late endosome–lysosome fusion and homotypic lysosome fusion in vitro. These studies indicate that: 1) fusion along the endocytic pathway is a highly regulated process, and 2) two SNARE molecules, Syntaxin 7 and human VAMP-7, are involved in fusion of vesicles in the late endocytic pathway in alveolar macrophages.

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Section: Discussionsupporting

confidence: 49%

Section: Discussionmentioning

confidence: 99%

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Syntaxin 7 and VAMP-7 are SolubleN-Ethylmaleimide–sensitive Factor Attachment Protein Receptors Required for Late Endosome–Lysosome and Homotypic Lysosome Fusion in Alveolar Macrophages

Ward

Pevsner

Scullion

et al. 2000

MBoC

128

116

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“…The distribution of syntaxin 7, in contrast, has been more controversial. In a variety of studies, syntaxin 7 has alternatively been placed in the early endosome (28,29), the late endosome (25), the late endosome and lysosome (18,26), or just the lysosome (24). The reasons for these discrepancies are not clear, but may reflect differences in methodologies, reagents, and cell type studies.…”

Section: Discussionmentioning

confidence: 93%

Syntaxins 13 and 7 Function at Distinct Steps During Phagocytosis

Collins

Schreiber

Grinstein

et al. 2002

The Journal of Immunology

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The phagosome is a dynamic organelle that undergoes progressive changes to acquire the machinery required to kill and degrade internalized foreign particles. This maturation process involves sequential interaction of newly formed phagosomes with several components of the endocytic pathway. The proteins that mediate the ordered fusion of endosomes and lysosomes with the phagosome are not known. In this study, we investigated the possible role of syntaxins present in the endo/lysosomal pathway in directing phagosomal maturation. We show that in phagocytic cells syntaxin 13 is localized to the recycling endosome compartment, while syntaxin 7 is found in late endosomes/lysosomes. Both proteins are recruited to the phagosome, but syntaxin 13 is acquired earlier and rapidly recycles off the phagosome, while syntaxin 7 is recruited later and continues to accumulate throughout the maturation process. Overexpression of truncated (cytosolic) forms of syntaxin 13 or 7 had no effect on phagocytosis, but exerted an inhibitory effect on phagosomal maturation. These results indicate that syntaxins 13 and 7 are both required for interaction of endosomes and/or lysosomes with the phagosome, but play distinct roles in the maturation process.

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“…Upon membrane contact, a specific SNARE complex in each organelle interacts with an opposing SNARE in another organelle to mediate membrane fusion. For example, it has been found that fusion between the late endosome and lysosome uses Syntaxin 7, Vti1b, and Syntaxin 8 on the late endosome and VAMP7 on the lysosome (4)(5)(6)(7)(8). In the autophagy pathway, it has been shown that VAMP7, VAMP8, and Vti1b play a role in autophagosome fusion in mammals (9)(10)(11).…”

mentioning

confidence: 99%

Phosphorylated Presenilin 1 decreases β-amyloid by facilitating autophagosome–lysosome fusion

Bustos

Pulina

Bispo

et al. 2017

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

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Presenilin 1 (PS1), the catalytic subunit of the γ-secretase complex, cleaves βCTF to produce Aβ. We have shown that PS1 regulates Aβ levels by a unique bifunctional mechanism. In addition to its known role as the catalytic subunit of the γ-secretase complex, selective phosphorylation of PS1 on Ser367 decreases Aβ levels by increasing βCTF degradation through autophagy. Here, we report the molecular mechanism by which PS1 modulates βCTF degradation. We show that PS1 phosphorylated at Ser367, but not nonphosphorylated PS1, interacts with Annexin A2, which, in turn, interacts with the lysosomal N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vamp8. Annexin A2 facilitates the binding of Vamp8 to the autophagosomal SNARE Syntaxin 17 to modulate the fusion of autophagosomes with lysosomes. Thus, PS1 phosphorylated at Ser367 has an antiamyloidogenic function, promoting autophagosome-lysosome fusion and increasing βCTF degradation. Drugs designed to increase the level of PS1 phosphorylated at Ser367 should be useful in the treatment of Alzheimer's disease.Presenilin 1 | phosphorylation | autophagy | autophagosome-lysosome fusion | Annexin A2

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Syntaxin 7 mediates endocytic trafficking to late endosomes

Cited by 37 publications

References 0 publications

Syntaxin 7 and VAMP-7 are SolubleN-Ethylmaleimide–sensitive Factor Attachment Protein Receptors Required for Late Endosome–Lysosome and Homotypic Lysosome Fusion in Alveolar Macrophages

Syntaxin 7 and VAMP-7 are SolubleN-Ethylmaleimide–sensitive Factor Attachment Protein Receptors Required for Late Endosome–Lysosome and Homotypic Lysosome Fusion in Alveolar Macrophages

Syntaxins 13 and 7 Function at Distinct Steps During Phagocytosis

Phosphorylated Presenilin 1 decreases β-amyloid by facilitating autophagosome–lysosome fusion

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