The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes

Chirivino, Dafne; Maestro, Laurence Del; Formstecher, Étienne; Hupé, Philippe; Raposo, Graça; Louvard, Daniel; Arpin, Monique

doi:10.1091/mbc.e10-09-0796

Cited by 51 publications

(53 citation statements)

References 40 publications

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“…Mutations in VPS41 can protect against a-synuclein-induced neurotoxicity in C. elegans and Parkinson's disease in mammalian model systems (Harrington et al, 2012;Ruan et al, 2010), and VPS41-deficient mouse embryos fail to develop beyond the gastrulation stage (Aoyama et al, 2012). In addition, the HOPS complex has been implicated in Ebola virus infection, EGFR trafficking, autophagolysosome formation and endosomal peptide loading of CD1d (Carette et al, 2011;Ganley et al, 2011;Chirivino et al, 2011;Garg et al, 2011). Mutations in the additional HOPS subunits VPS33b and SPE-39 cause complex multiorgan failures such as ARC syndrome, which is characterized by impairments in granule secretion and membrane fusion (Gissen et al, 2004;Cullinane et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

“…Despite significant evolutionary conservation of the actual tethering complex from yeast to human, the current understanding of the HOPS complex composition, recruitment and function in mammalian systems remains limited. Human HOPS has been implicated in EGFR routing (Chirivino et al, 2011) and autophagosome maturation (Liang et al, 2008), and is critical for efficient cytosolic entry of Ebola virus from NPC-1 containing late endosomes (Carette et al, 2011). Mutations in the additional HOPS subunits VPS33b and SPE-39 cause complex multiorgan failures, such as ARC syndrome, which is characterized by impairments in granule secretion and membrane fusion (Gissen et al, 2004;Cullinane et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L

Kant

Fish

Janssen

et al. 2013

Journal of Cell Science

166

161

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SummaryLate endosomes and lysosomes are dynamic organelles that constantly move and fuse to acquire cargo from early endosomes, phagosomes and autophagosome. Defects in lysosomal dynamics cause severe neurodegenerative and developmental diseases, such as Niemann-Pick type C disease and ARC syndrome, yet little is known about the regulation of late endosomal fusion in a mammalian system. Mammalian endosomes destined for fusion need to be transported over very long distances before they tether to initiate contact. Here, we describe that lysosomal tethering and transport are combined processes co-regulated by one multi-protein complex: RAB7-RILP-ORP1L. We show that RILP directly and concomitantly binds the tethering HOPS complex and the p150Glued subunit of the dynein motor. ORP1L then functions as a cholesterol-sensing switch controlling RILP-HOPS-p150Glued interactions. We show that RILP and ORP1L control Ebola virus infection, a process dependent on late endosomal fusion. By combining recruitment and regulation of both the dynein motor and HOPS complex into a single multiprotein complex, the RAB7-RILP-ORP1L complex efficiently couples and regulates the timing of microtubule minus-end transport and fusion, two major events in endosomal biology.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L

Kant

Fish

Janssen

et al. 2013

Journal of Cell Science

166

161

View full text Add to dashboard Cite

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“…The organization of these mammalian complexes has only partly been addressed with seemingly conflicting results and hampered the interpretation of functional experiments in which the roles of specific or multiple units are addressed (17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27). Furthermore, it is not known what drives membrane specificity of these complexes in mammals.…”

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confidence: 99%

Characterization of the Mammalian CORVET and HOPS Complexes and Their Modular Restructuring for Endosome Specificity

Kant

Jonker

Wijdeven

et al. 2015

Journal of Biological Chemistry

117

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Background:The CORVET and HOPS complexes regulate endosomal cargo trafficking but have not been well characterized in mammals. Results: A detailed analysis of subunit interactions within the mammalian CORVET, HOPS, and VIPAS39/VPS33B complexes. Conclusion: Tethering complexes have adapted to the higher complexity of trafficking in mammalian cells. Significance: This work provides a detailed architectural insight into the mammalian endosomal tethering complexes.

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“…For example, degradation of the EGF receptor is dramatically reduced by depletion of Vps11 [19]. Depletion of SPE-39 induced a delay in the downregulation of the EGF receptor 30 min after the addition of EGF.…”

Section: Discussionmentioning

confidence: 99%

Inhibitory effect of SPE‐39 due to tyrosine phosphorylation and ubiquitination on the function of Vps33B in the EGF‐stimulated cells

et al. 2012

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a b s t r a c tAlthough SPE-39 is a binding protein to Vps33B that is one of the subunit in the mammalian HOPS complex, the elements of SPE-39 function remain unknown. Here, we show that tyrosine phosphorylation of SPE-39 following EGF stimulation plays a role in the stability of SPE-39 itself. Ubiquitination of the C-terminal region of SPE-39 was also elevated in response to EGF stimulation, and this process was regulated by the phosphorylation of Tyr-11 in SPE-39. However, association of Vps33B with SPE-39 inhibited the elevation of ubiquitination of SPE-39 following EGF stimulation, which might be responsible for the stabilization of SPE-39. Furthermore, an opposing functional relationship between SPE-39 and Vps33B on the downregulation of the EGF receptor was observed in EGFstimulated COS-7 cells. Structured summary of protein interactions:Vps33B and EGFR colocalize by fluorescence microscopy (View interaction) Vps33B and SPE-39 physically interact by anti bait coimmunoprecipitation (View interaction) Vps33B and SPE-39 physically interact by anti tag coimmunoprecipitation (View interaction) Vps33B and SPE-39 colocalize by fluorescence microscopy (View interaction)

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The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes

Cited by 51 publications

References 40 publications

Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L

Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L

Characterization of the Mammalian CORVET and HOPS Complexes and Their Modular Restructuring for Endosome Specificity

Inhibitory effect of SPE‐39 due to tyrosine phosphorylation and ubiquitination on the function of Vps33B in the EGF‐stimulated cells

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