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CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling

CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling

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GENAU, Heide Marika, Jessica HUBER, Francesco BASCHIERI, Masato AKUTSU, Volker DÖTSCH, Hesso FARHAN, Vladimir ROGOV, Christian BEHRENDS, 2015. CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling. In: Molecular Cell. 57(6), pp. 995-1010. ISSN 1097-2765. eISSN 1097-4164

@article{Genau2015CUL3--30895, title={CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling}, year={2015}, doi={10.1016/j.molcel.2014.12.040}, number={6}, volume={57}, issn={1097-2765}, journal={Molecular Cell}, pages={995--1010}, author={Genau, Heide Marika and Huber, Jessica and Baschieri, Francesco and Akutsu, Masato and Dötsch, Volker and Farhan, Hesso and Rogov, Vladimir and Behrends, Christian} }

Farhan, Hesso Huber, Jessica Akutsu, Masato Dötsch, Volker Huber, Jessica Dötsch, Volker CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling Rogov, Vladimir 2015-05-06T09:45:29Z Behrends, Christian Rogov, Vladimir Behrends, Christian eng Baschieri, Francesco 2015-05-06T09:45:29Z 2015 Farhan, Hesso Akutsu, Masato Genau, Heide Marika Baschieri, Francesco Genau, Heide Marika The small Rho GTPase RAC1 is an essential regulator of cellular signaling that controls actin rearrangements and cell motility. Here, we identify a novel CUL3 RING ubiquitin ligase complex, containing the substrate adaptors KBTBD6 and KBTBD7, that mediates ubiquitylation and proteasomal degradation of TIAM1, a RAC1-specific GEF. Increasing the abundance of TIAM1 by depletion of KBTBD6 and/or KBTBD7 leads to elevated RAC1 activity, changes in actin morphology, loss of focal adhesions, reduced proliferation, and enhanced invasion. KBTBD6 and KBTBD7 employ ATG8 family-interacting motifs to bind preferentially to GABARAP proteins. Surprisingly, ubiquitylation and degradation of TIAM1 by CUL3KBTBD6/KBTBD7 depends on its binding to GABARAP proteins. Our study reveals that recruitment of CUL3<sup>KBTBD6/KBTBD7</sup> to GABARAP-containing vesicles regulates the abundance of membrane-associated TIAM1 and subsequently spatially restricted RAC1 signaling. Besides their role in autophagy and trafficking, we uncovered a previously unknown function of GABARAP proteins as membrane-localized signaling scaffolds.

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