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    Structural and functional analysis of the GABARAP interaction motif (GIM)

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    64
    Author
    Rogov, VV; Stolz, A; Ravichandran, AC; Rios-Szwed, DO; Suzuki, H; Kniss, A; Loehr, F; Wakatsuki, S; Doetsch, V; Dikic, I; ...
    Date
    2017-08-01
    Source Title
    EMBO Reports
    Publisher
    WILEY
    University of Melbourne Author/s
    Dobson, Renwick
    Affiliation
    Biochemistry and Molecular Biology
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Rogov, V. V., Stolz, A., Ravichandran, A. C., Rios-Szwed, D. O., Suzuki, H., Kniss, A., Loehr, F., Wakatsuki, S., Doetsch, V., Dikic, I., Dobson, R. C. J. & McEwan, D. G. (2017). Structural and functional analysis of the GABARAP interaction motif (GIM). EMBO REPORTS, 18 (8), pp.1382-1396. https://doi.org/10.15252/embr.201643587.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/259589
    DOI
    10.15252/embr.201643587
    Abstract
    Through the canonical LC3 interaction motif (LIR), [W/F/Y]-X1-X2-[I/L/V], protein complexes are recruited to autophagosomes to perform their functions as either autophagy adaptors or receptors. How these adaptors/receptors selectively interact with either LC3 or GABARAP families remains unclear. Herein, we determine the range of selectivity of 30 known core LIR motifs towards individual LC3s and GABARAPs. From these, we define a G ABARAP I nteraction M otif (GIM) sequence ([W/F]-[V/I]-X2-V) that the adaptor protein PLEKHM1 tightly conforms to. Using biophysical and structural approaches, we show that the PLEKHM1-LIR is indeed 11-fold more specific for GABARAP than LC3B. Selective mutation of the X1 and X2 positions either completely abolished the interaction with all LC3 and GABARAPs or increased PLEKHM1-GIM selectivity 20-fold towards LC3B. Finally, we show that conversion of p62/SQSTM1, FUNDC1 and FIP200 LIRs into our newly defined GIM, by introducing two valine residues, enhances their interaction with endogenous GABARAP over LC3B. The identification of a GABARAP-specific interaction motif will aid the identification and characterization of the expanding array of autophagy receptor and adaptor proteins and their in vivo functions.

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