The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.
The endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray ... crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). NMR analysis shows that each of the three rigidly arranged overlapping UBAs making up the SOUBA interact with ubiquitin. We demonstrate that UBAP1-containing ESCRT-I is essential for degradation of antiviral cell-surface proteins, such as tetherin (BST-2/CD317), by viral countermeasures, namely, the HIV-1 accessory protein Vpu and the Kaposi sarcoma-associated herpesvirus (KSHV) ubiquitin ligase K5.
Mesh Terms:
Amino Acid Sequence, Antigens, CD, Carrier Proteins, Chromatography, Gel, Crystallography, X-Ray, Endosomal Sorting Complexes Required for Transport, GPI-Linked Proteins, Human Immunodeficiency Virus Proteins, Humans, Immediate-Early Proteins, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Structure, Tertiary, Ubiquitin, Viral Regulatory and Accessory Proteins
Amino Acid Sequence, Antigens, CD, Carrier Proteins, Chromatography, Gel, Crystallography, X-Ray, Endosomal Sorting Complexes Required for Transport, GPI-Linked Proteins, Human Immunodeficiency Virus Proteins, Humans, Immediate-Early Proteins, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Structure, Tertiary, Ubiquitin, Viral Regulatory and Accessory Proteins
Structure
Date: Mar. 07, 2012
PubMed ID: 22405001
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