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    Missing-in-metastasis protein downregulates CXCR4 by promoting ubiquitylation and interaction with small Rab GTPases

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    Author
    Li, L.
    Baxter, S.S.
    Gu, N.
    Date
    2017
    Journal
    Journal of Cell Science
    Publisher
    Company of Biologists Ltd
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://www.doi.org/10.1242/jcs.198937
    Abstract
    Surface expression of chemokine receptor CXCR4 is downregulated by missing-in-metastasis protein (MIM; also known as MTSS1), a member of the inverse BAR (I-BAR)-domain protein family that recognizes and generates membranes with negative curvature. Yet, the mechanism for the regulation is unknown. Here, we show that MIM forms a complex with CXCR4 by binding to E3 ubiquitin ligase AIP4 (also known as ITCH) in response to stromal cell-derived factor 1 (SDF-1; also known as CXCL12). Overexpression of MIM promoted CXCR4 ubiquitylation, inhibited cellular response to SDF-1, caused accumulation and aggregation of multivesicular bodies (MVBs) in the cytoplasm, and promoted CXCR4 sorting into MVBs in a manner depending on binding to AIP4. In response to SDF-1, MIM also bound transiently to the small GTPase Rab5 at 5 min and to Rab7 at 30 min. Binding to Rab7 requires an N-terminal coiled-coil motif, deletion of which abolished MIM-mediated MVB formation and CXCR4 internalization. Our results unveil a previously unknown property of MIM that establishes the linkage of protein ubiquitylation with Rab-guided trafficking of CXCR4 in endocytic vesicles. Copyright 2017. Published by The Company of Biologists Ltd.
    Keyword
    AIP4
    CXCR4
    MIM
    MVBs
    Rab7
    Ubiquitylation
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85017542196&doi=10.1242%2fjcs.198937&partnerID=40&md5=de3ac4e41884482f909822b5cbecc3e6; http://hdl.handle.net/10713/9949
    ae974a485f413a2113503eed53cd6c53
    10.1242/jcs.198937
    Scopus Count
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    UMB Open Access Articles 2017

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