Assembly of the AAA ATPase Vps4 on ESCRT-III

Shestakova, Anna; Hanono, Abraham; Drosner, Stacey; Curtiss, Matt; Davies, Brian A.; Katzmann, David J.; Babst, Markus

doi:10.1091/mbc.e09-07-0572

Cited by 99 publications

(140 citation statements)

References 57 publications

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“…Nevertheless, our data are consistent with published models in which LIP5 and CHMP5 are initially tightly associated in the cytoplasm (53). Formation of stable ESCRT-III-associated LIP5-VPS4 complexes might then require both a direct LIP5(VSL)-VPS4(SAB) interaction and a supporting interaction between the CHMP1B MIM1 element and the first LIP5 MIT domain (33,45). It is not yet clear why CHMP5 is also required to form this complex, but it was recently shown that CHMP5 can bind the ALIX paralog BROX at a site located just downstream of the LIP5-binding site (77).…”

Section: Discussionsupporting

confidence: 92%

“…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%

“…VPS4 enzymes are recruited to their sites of action, at least in part, by binding to a variety of different and often partially redundant MIM elements that are exposed upon ESCRT-III filament formation (19,(32)(33)(34)(35)(36)(37)(38). In addition to these general ESCRT-III interactions, two binary complexes, CHMP1-IST1 and LIP5-CHMP5, play particularly important roles in VPS4 recruitment and activation.…”

mentioning

confidence: 99%

“…These two complexes appear to act synergistically because they exhibit synthetic multivesicular body sorting phenotypes in Saccharomyces cerevisiae (51,52). Moreover, the tandem MIT domains within LIP5 can bind MIM elements within both CHMP1 and IST1, implying that the complexes probably interact directly in cells (12,33,34,41,42).…”

mentioning

confidence: 99%

“…This assembly then recruits Vta1p, which helps to promote assembly of the active Vps4p enzyme (33). It is not yet clear precisely how Vps60p/CHMP5 fits into this scheme, but a leading model is that Vps60p acts through Vta1p very late in the process to help stimulate Vps4p to recycle ESCRT components back into the cytoplasm (34).…”

mentioning

confidence: 99%

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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: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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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Plant endosomes as protein sorting hubs

2022

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Endocytosis, secretion, and endosomal trafficking are key cellular processes that control the composition of the plasma membrane. Through the coordination of these trafficking pathways, cells can adjust the composition, localization, and turnover of proteins and lipids in response to developmental or environmental cues. Upon being incorporated into vesicles and internalized through endocytosis, plant plasma membrane proteins are delivered to the trans-Golgi network (TGN). At the TGN, plasma membrane proteins are recycled back to the plasma membrane or transferred to multivesicular endosomes (MVEs), where they are further sorted into intralumenal vesicles for degradation in the vacuole. Both types of plant endosomes, TGN and MVEs, act as sorting organelles for multiple endocytic, recycling, and secretory pathways. Molecular assemblies such as retromer, ESCRT (endosomal sorting complex required for transport) machinery, small GTPases, adaptor proteins, and SNAREs associate with specific domains of endosomal membranes to mediate different sorting and membrane-budding events. In this review, we discuss the mechanisms underlying the recognition and sorting of proteins at endosomes, membrane remodeling and budding, and their implications for cellular trafficking and physiological responses in plants.

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Guidelines for the purification and characterization of extracellular vesicles of parasites

Fernandez‐Becerra,

Xander,

Alfandari

et al. 2023

J of Extracellular Bio

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Parasites are responsible for the most neglected tropical diseases, affecting over a billion people worldwide (WHO, 2015) and accounting for billions of cases a year and responsible for several millions of deaths. Research on extracellular vesicles (EVs) has increased in recent years and demonstrated that EVs shed by pathogenic parasites interact with host cells playing an important role in the parasite's survival, such as facilitation of infection, immunomodulation, parasite adaptation to the host environment and the transfer of drug resistance factors. Thus, EVs released by parasites mediate parasite‐parasite and parasite‐host intercellular communication. In addition, they are being explored as biomarkers of asymptomatic infections and disease prognosis after drug treatment. However, most current protocols used for the isolation, size determination, quantification and characterization of molecular cargo of EVs lack greater rigor, standardization, and adequate quality controls to certify the enrichment or purity of the ensuing bioproducts. We are now initiating major guidelines based on the evolution of collective knowledge in recent years. The main points covered in this position paper are methods for the isolation and molecular characterization of EVs obtained from parasite‐infected cell cultures, experimental animals, and patients. The guideline also includes a discussion of suggested protocols and functional assays in host cells

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Assembly of the AAA ATPase Vps4 on ESCRT-III

Abstract: A complex network of interactions mediates the recruitment of Vps4 to ESCRT-III and its subsequent assembly, two key steps in the ESCRT-dependent vesicle formation at the endosome. A model is presented depicting the order of events that lead to active, ESCRT-III–associated Vps4.

Cited by 99 publications

References 57 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

Plant endosomes as protein sorting hubs

Guidelines for the purification and characterization of extracellular vesicles of parasites

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