Structural Basis for Endosomal Targeting by the Bro1 Domain

Kim, Jaewon; Sitaraman, Sujatha; Hierro, Aitor; Beach, Bridgette M.; Odorizzi, Greg; Hurley, James H.

doi:10.1016/j.devcel.2005.04.001

Cited by 174Cellular transport and secretionUbiquitin and proteasome pathwaysAutophagy in Disease and Therapy

Structural Basis for Endosomal Targeting by the Bro1 Domain

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Kim, Jaewon, Sitaraman, Sujatha, Hierro, Aitor, Beach, Bridgette M., Odorizzi, Greg, Hurley, James H.·2005·Developmental Cell

DOI 10.1016/j.devcel.2005.04.001PMC PMC2862258

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Abstract

Proteins delivered to the lysosome or the yeast vacuole via late endosomes are sorted by the ESCRT complexes and by associated proteins, including Alix and its yeast homolog Bro1. Alix, Bro1, and several other late endosomal proteins share a conserved 160 residue Bro1 domain whose boundaries, structure, and function have not been characterized. The crystal structure of the Bro1 domain of Bro1 reveals a folded core of 367 residues. The extended Bro1 domain is necessary and sufficient for binding to the ESCRT-III subunit Snf7 and for the recruitment of Bro1 to late endosomes. The structure resembles a boomerang with its concave face filled in and contains a triple tetratricopeptide repeat domain as a substructure. Snf7 binds to a conserved hydrophobic patch on Bro1 that is required for protein complex formation and for the protein-sorting function of Bro1. These results define a conserved mechanism whereby Bro1 domain-containing proteins are targeted to endosomes by Snf7 and its orthologs.

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Molecular Architecture and Functional Model of the Complete Yeast ESCRT-I Heterotetramer
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Beyond Tsg101: the role of Alix in 'ESCRTing' HIV-1
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Human ESCRT-II Complex and Its Role in Human Immunodeficiency Virus Type 1 Release
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Structural basis for viral late-domain binding to Alix
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The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis
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The ESCRT pathway and HIV-1 budding
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Molecular mechanisms of late endosome morphology, identity and sorting
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An Alix Fragment Potently Inhibits HIV-1 Budding
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ESCRT-III-Associated Protein ALIX Mediates High-Affinity Phosphate Transporter Trafficking to Maintain Phosphate Homeostasis in Arabidopsis
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Endocytic pathway is required for Drosophila Toll innate immune signaling
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Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT-independent manner
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ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis
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Control of Bro1-Domain Protein Rim20 Localization by External pH, ESCRT Machinery, and theSaccharomyces cerevisiaeRim101 Pathway
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Scratching the niche that controls Caenorhabditis elegans germline stem cells
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LIN-12/Notch trafficking and regulation of DSL ligand activity during vulval induction in Caenorhabditis elegans
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An ordered pathway for the assembly of ESCRT-containing fungal ambient pH signalling complexes at the plasma membrane
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Arabidopsis ALIX is required for the endosomal localization of the deubiquitinating enzyme AMSH3
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Involvement of the Conserved Adaptor Protein Alix in Actin Cytoskeleton Assembly
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Further Characterization of the Signaling Proteolysis Step in theAspergillus nidulanspH Signal Transduction Pathway
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A Novel Requirement for C. elegans Alix/ALX-1 in RME-1-Mediated Membrane Transport
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Proline‐Rich Regions and Motifs in Trafficking: From ESCRT Interaction to Viral Exploitation
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New component of ESCRT-I regulates endosomal sorting complex assembly
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Cell entry and release of quasi-enveloped human hepatitis viruses
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Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles
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ESCRT & Co
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HD-PTP and Alix share some membrane-traffic related proteins that interact with their Bro1 domains or proline-rich regions
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Basic Residues in the Nucleocapsid Domain of Gag Are Critical for Late Events of HIV-1 Budding
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The Crystal Structure of the C‐Terminal Domain of Vps28 Reveals a Conserved Surface Required for Vps20 Recruitment
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Ubiquitin recognition in endocytic trafficking – with or without ESCRT-0
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Myopic acts in the endocytic pathway to enhance signaling by the Drosophila EGF receptor
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Why Cells and Viruses Cannot Survive without an ESCRT
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A Screen for Conditional Growth Suppressor Genes Identifies the Drosophila Homolog of HD-PTP as a Regulator of the Oncoprotein Yorkie
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Activation of the Retroviral Budding Factor ALIX
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A genome-wide deletion mutant screen identifies pathways affected by nickel sulfate in Saccharomyces cerevisiae
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The ESCRT-III machinery participates in the production of extracellular vesicles and protein export during Plasmodium falciparum infection
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ALG-2 interacting protein-X (Alix) is essential for clathrin-independent endocytosis and signaling
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ESCRT machinery components are required for Orthobunyavirus particle production in Golgi compartments
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SRP RNA Remodeling by SRP68 Explains Its Role in Protein Translocation
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Vesicle formation within endosomes: An ESCRT marks the spot
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Interaction of HIV-1 Nef Protein with the Host Protein Alix Promotes Lysosomal Targeting of CD4 Receptor
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Comprehensive analysis of the human ESCRT-III-MIT domain interactome reveals new cofactors for cytokinetic abscission
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Dynamics of ESCRT proteins
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Identification of the HIV-1 NC Binding Interface in Alix Bro1 Reveals a Role for RNA
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Phosphorylation-Dependent Activation of the ESCRT Function of ALIX in Cytokinetic Abscission and Retroviral Budding
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Budding of a Retrovirus: Some Assemblies Required
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Alix Protein Is Substrate of Ozz-E3 Ligase and Modulates Actin Remodeling in Skeletal Muscle
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ESCRT‐II functions by linking to ESCRT‐I in human immunodeficiency virus‐1 budding
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The Phe105 Loop of Alix Bro1 Domain Plays a Key Role in HIV-1 Release
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HIV-1 Nucleocapsid Mimics the Membrane Adaptor Syntenin PDZ to Gain Access to ESCRTs and Promote Virus Budding
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The Bro1 domain-containing Myopic/HDPTP coordinates with Rab4 to regulate cell adhesion and migration
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NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z
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Structure of the Bro1 Domain Protein BROX and Functional Analyses of the ALIX Bro1 Domain in HIV-1 Budding
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The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis
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Authors: Kim, J., Sitaraman, S., Hierro, A., Beach, B. M., Odorizzi, G., & Hurley, J. H.
Affiliations: National Institutes of Health (US)
University of Colorado Boulder (US)
Corresponding author: Hurley, James H.
ORCID: Kim, Jaewon
Hierro, Aitor
Beach, Bridgette M.
Odorizzi, Greg
Hurley, James H.
Venue: Developmental Cell
Publisher: Elsevier BV
Published: 2005-06
Volume: 8
Issue: 6
Pages: 937-947
ISSN: 1534-5807 (ISSN-L)
DOI: 10.1016/j.devcel.2005.04.001
PMC: PMC2862258
OpenAlex: W2033191472
Cited by: 174
References: 70
Citations by year: 2026: 3 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 4 · 2021: 8 · 2020: 8 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 9 · 2015: 6 · 2014: 8 · 2013: 11 · 2012: 12
FWCI: 7.07
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2968 d)
Locations: Developmental Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R01GM065505, GM065505)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords: Bro1 domain, Snf7, ESCRT-III, lysosomal targeting, Alix, tetratricopeptide repeats, protein sorting, crystal structure, hydrophobic patch, yeast vacuole
MeSH terms: Animals, Cytoplasm, Fluorescent Antibody Technique, Fungal Proteins, Models, Molecular, Molecular Sequence Data, Protein Binding, Endosomes, Gene Expression Regulation, Fungal, Mutagenesis, Protein Structure, Tertiary, Crystallography, X-Ray, Protein Transport, Protein Interaction Mapping, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Structural Homology, Protein, Green Fluorescent Proteins, Endosomal Sorting Complexes Required for Transport, In Vitro Techniques

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Structural Basis for Endosomal Targeting by the Bro1 Domain

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