Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes

Nickerson, Daniel P.; West, Matthew; Odorizzi, Greg

doi:10.1083/jcb.200606113

Cited by 146 publications

(209 citation statements)

References 21 publications

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“…Our mutational and NMR spectroscopic data are consistent with a model in which the terminal helix of CHMP1B makes a MIM1-like interaction with the helix 2/3 groove of the first LIP5 MIT module. CHMP1B/Did2p is an unusual ESCRT-III protein in that it binds well to the MIT domains from both VPS4 and LIP5 (33,34,39,40,50,58). This is apparently possible because the helix 2/3 grooves of the MIT domains from VPS4 and LIP5 are similar in character.…”

Section: Discussionmentioning

confidence: 99%

Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport

Skalicky¹,

Arii²,

Wenzel³

et al. 2012

Journal of Biological Chemistry

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Background: LIP5 helps regulate the membrane fission and recycling activities of the ESCRT pathway. Results: Biochemical and structural studies reveal how LIP5 binds different ESCRT-III proteins. Conclusion: ESCRT-III proteins bind independently to different LIP5 sites, and the LIP5-CHMP5 structure reveals a novel interaction mode. Significance: The results help explain how LIP5 can activate VPS4 ATPases to act on ESCRT-III filaments.

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Section: Discussionmentioning

confidence: 99%

Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport

Skalicky¹,

Arii²,

Wenzel³

et al. 2012

Journal of Biological Chemistry

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“…28,36 This result suggests that Vps4 activity is necessary for cargo transport and for removal of the ESCRT machinery from the endosomal membrane. However, even though dissociation of ESCRT-III is essential for sorting, it is not a prerequisite for luminal vesicle formation, 37 and for uncoupling MVB cargo sorting from the budding of vesicles into the endosomal lumen.…”

Section: Biogenesis Of Mvbsmentioning

confidence: 99%

Autophagy and multivesicular bodies: two closely related partners

2008

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In the majority of cell types, multivesicular bodies (MVBs) are a special kind of late endosomes, crucial intermediates in the internalization of nutrients, ligands and receptors through the endolysosomal system. ESCRT-0, I, II and III (endosomal sorting complex required for transport) are involved in the sorting of proteins into MVBs, generating the intraluminal vesicles. Autophagy is a lysosomal degradation pathway for cytoplasmic components such as proteins and organelles. The autophagosome, a well-characterized structure of the autophagy pathway, can fuse with endocytic structures such as MVBs to generate the amphisome. Finally, the amphisome fuses with the lysosome to degrade the material wrapped inside. Currently, clear evidence suggests that efficient autophagic degradation requires functional MVBs. This review highlights the most recent advances in our understanding of the molecular machinery that participates in MVB biogenesis and regulates the interplay between autophagy and this organelle.

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“…Establishment of an in Vitro Biochemical Assay System for MVB Formation-In previous MVB studies, internal vesicles in the endosomes have been observed by electron microscopy (EM) (15,38). However, quantification of MVB formation by EM analysis is limited.…”

Section: Endosomal Na ϩ /H ϩ Exchange Activity Is Required For Efficimentioning

confidence: 99%

The Endosomal Na+/H+ Exchanger Contributes to Multivesicular Body Formation by Regulating the Recruitment of ESCRT-0 Vps27p to the Endosomal Membrane

Mitsui

Koshimura

Yoshikawa

et al. 2011

Journal of Biological Chemistry

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Multivesicular bodies (MVBs) are late endosomal compartments containing luminal vesicles (MVB vesicles) that are formed by inward budding of the endosomal membrane. In budding yeast, MVBs are an important cellular mechanism for the transport of membrane proteins to the vacuolar lumen. This process requires a class E subset of vacuolar protein sorting (VPS) genes. VPS44 (allelic to NHX1) encodes an endosomelocalized Na ؉ /H ؉ exchanger. The function of the VPS44 exchanger in the context of vacuolar protein transport is largely unknown. Using a cell-free MVB formation assay system, we demonstrated that Nhx1p is required for the efficient formation of MVB vesicles in the late endosome. The recruitment of Vps27p, a class E Vps protein, to the endosomal membrane was dependent on Nhx1p activity and was enhanced by an acidic pH at the endosomal surface. Taken together, we propose that Nhx1p contributes to MVB formation by the recruitment of Vps27p to the endosomal membrane, possibly through Nhx1p antiporter activity.Multivesicular bodies (MVBs) 3 are a subset of late endosomes that contain internal vesicles, permitting precursor and plasma membrane proteins to reach the lysosome or vacuole lumen for degradation or maturation, respectively. In eukaryotic cells, the MVB pathway controls various important processes such as receptor down-regulation, antigen presentation, cytokinesis, retroviral budding, and autophagy (1-6). In the budding yeast Saccharomyces cerevisiae, previous studies identified a number of genes involved in vacuolar protein sorting (VPS) (7,8). These Vps proteins function at distinct steps of protein transport between the Golgi complex and the vacuole (7,8). A subset of Vps proteins, class E proteins, is involved in MVB formation. Most class E proteins are components of five distinct complexes; Vps27p-Hse1p (also called endosomal sorting complexes required for transport-0 (ESCRT-0), -I, -II, and -III and Vps4p. These complexes are required for the formation of internal vesicles and sorting of cargo proteins to the vesicles from the endosomal membrane (3, 9). Vps27p (ESCRT-0) recruits ESCRT-I, which in turn recruits and/or activates ESCRT-II and ESCRT-III at the endosome (3, 10). Recent in vitro studies have provided new insights into the precise role of each ESCRT complex in MVB formation (11-13). ESCRT-0 initiates the MVB sorting process by recruiting ESCRT-I to the endosomal membrane and concentrating ubiquitylated MVB cargos to the vesicle budding site (12). ESCRT-I and ESCRT-II are directly involved in membrane budding by stabilizing the bud necks, whereas ESCRT-III is responsible for the cleavage of bud necks (11-13). Finally, the AAA-type ATPase Vps4p dissociates the ESCRT-III complex from the endosome (14). The sequential activity of these complexes on the cytoplasmic surface of endosomes directs the budding and fission of vesicles into the lumen of the endosome and the sequestration of cargo proteins in the vesicle. Defects in ESCRT proteins prevent internal vesicle formation and result in exagg...

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Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes

Cited by 146 publications

References 21 publications

Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport

Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport

Autophagy and multivesicular bodies: two closely related partners

The Endosomal Na+/H+ Exchanger Contributes to Multivesicular Body Formation by Regulating the Recruitment of ESCRT-0 Vps27p to the Endosomal Membrane

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