ArticleStructure (London, England : 1993)2011
Structural basis for ESCRT-III CHMP3 recruitment of AMSH.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- The green ESCRTs: Newly defined roles for ESCRT proteins in plants.The Journal of biological chemistry · 2025Review
- Article
- Structural and Functional Basis of JAMM Deubiquitinating Enzymes in Disease.Biomolecules · 2022Review
- A necroptosis -related signature for predicting prognosis and immunotherapy in hepatocellular carcinoma.Frontiers in genetics · 2022Article
- Crystallization and Biophysical Approaches for Studying the Interactions Between the Vps4-MIT Domain and ESCRT-III Proteins.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Structures, Functions, and Dynamics of ESCRT-III/Vps4 Membrane Remodeling and Fission Complexes.Annual review of cell and developmental biology · 2018Review
- CHMP1B is a target of USP8/UBPY regulated by ubiquitin during endocytosis.PLoS genetics · 2018Article
- Structural basis of katanin p60:p80 complex formation.Scientific reports · 2017Article
- Reverse-topology membrane scission by the ESCRT proteins.Nature reviews. Molecular cell biology · 2017Review
- NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.Scientific reports · 2016Article
- Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.Journal of molecular biology · 2016Review
- A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum-infected erythrocytes.Blood · 2016Article
- Dynamics of an Active-Site Flap Contributes to Catalysis in a JAMM Family Metallo Deubiquitinase.Biochemistry · 2015Article
- Distinct mechanisms of recognizing endosomal sorting complex required for transport III (ESCRT-III) protein IST1 by different microtubule interacting and trafficking (MIT) domains.The Journal of biological chemistry · 2015Article
- Review
- Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and product.Biochemistry · 2014Article
- Vfa1 binds to the N-terminal microtubule-interacting and trafficking (MIT) domain of Vps4 and stimulates its ATPase activity.The Journal of biological chemistry · 2014Article
- The ESCRT-deubiquitinating enzyme USP8 in the cervical spinal cord of wild-type and Vps54-recessive (wobbler) mutant mice.Histochemistry and cell biology · 2014Article
- Mechanism of recruitment and activation of the endosome-associated deubiquitinase AMSH.Biochemistry · 2013Article
- Doa4 function in ILV budding is restricted through its interaction with the Vps20 subunit of ESCRT-III.Journal of cell science · 2013Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Endosomal sorting complexes required for transport (ESCRT) recognize ubiquitinated cargo and catalyze diverse budding processes including multivesicular body biogenesis, enveloped virus egress, and cytokinesis. We present the crystal structure of an N-terminal fragment of the deubiquitinating enzyme AMSH (AMSHΔC) in complex with the C-terminal region of ESCRT-III CHMP3 (CHMP3ΔN). AMSHΔC folds into an elongated 90 Å long helical assembly that includes an unusual MIT domain. CHMP3ΔN is unstructured in solution and helical in complex with AMSHΔC, revealing a novel MIT domain interacting motif (MIM) that does not overlap with the CHMP1-AMSH binding site. ITC and SPR measurements demonstrate an unusual high-affinity MIM-MIT interaction. Structural analysis suggests a regulatory role for the N-terminal helical segment of AMSHΔC and its destabilization leads to a loss of function during HIV-1 budding. Our results indicate a tight coupling of ESCRT-III CHMP3 and AMSH functions and provide insight into the regulation of ESCRT-III.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.