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Mol Biol Cell ; 28(2): 309-321, 2017 01 15.
Artigo em Inglês | MEDLINE | ID: mdl-27881666

RESUMO

Lysosomal membrane fusion mediates the last step of the autophagy and endocytosis pathways and supports organelle remodeling and biogenesis. Because fusogenic proteins and lipids concentrate in a ring at the vertex between apposing organelle membranes, the encircled area of membrane can be severed and internalized within the lumen as a fragment upon lipid bilayer fusion. How or why this intralumenal fragment forms during fusion, however, is not entirely clear. To better understand this process, we studied fragment formation during homotypic vacuolar lysosome membrane fusion in Saccharomyces cerevisiae Using cell-free fusion assays and light microscopy, we find that GTPase activation and trans-SNARE complex zippering have opposing effects on fragment formation and verify that this affects the morphology of the fusion product and regulates transporter protein degradation. We show that fragment formwation is limited by stalk expansion, a key intermediate of the lipid bilayer fusion reaction. Using electron microscopy, we present images of hemifusion diaphragms that form as stalks expand and propose a model describing how the fusion machinery regulates fragment formation during lysosome fusion to control morphology and protein lifetimes.


Assuntos
Fusão de Membrana/fisiologia , Proteínas de Transporte/metabolismo , Ativadores de GTP Fosfo-Hidrolase/metabolismo , Membranas Intracelulares/metabolismo , Bicamadas Lipídicas/metabolismo , Proteínas de Membrana Lisossomal/metabolismo , Lisossomos/metabolismo , Membranas/metabolismo , Proteínas SNARE/metabolismo , Saccharomyces cerevisiae/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Vacúolos/metabolismo
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