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Probing the DCAF12 interactions with MAGEA3 and CCT5 C-terminal degrons

by Seitova, Alma , Brazeau, Jean-Francois , Loppnau, Peter , Szewczyk, Magdalena , Barsyte-Lovejoy, Dalia , Santhakumar, Vijayaratnam , Duda, David , Vu, Victoria , Li, Yanjun , Mei, Tony , Li, Yen-Yen , Righetto, Germanna Lima , Zeng, Hong , Halabelian, Levon , Chaudhry, Charu , Yin, Yanting

in Biochemistry

2023

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Probing the DCAF12 interactions with MAGEA3 and CCT5 C-terminal degrons

in Biochemistry

2023

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Paper

Probing the DCAF12 interactions with MAGEA3 and CCT5 C-terminal degrons

Seitova, Alma,

Brazeau, Jean-Francois,

Loppnau, Peter,

Szewczyk, Magdalena,

Barsyte-Lovejoy, Dalia,

Santhakumar, Vijayaratnam,

Duda, David,

Vu, Victoria,

Li, Yanjun,

Mei, Tony,

Li, Yen-Yen,

Righetto, Germanna Lima,

Zeng, Hong,

Halabelian, Levon,

Chaudhry, Charu,

Yin, Yanting

2023

Overview

DCAF12 is the substrate recognition component of the CRL4 E3 ligase complex that can recognize C-terminal double-glutamic acid degrons to promote degradation of its cognate substrates via the ubiquitin proteasome system. MAGEA3 and CCT5 proteins were reported to be cellular targets of DCAF12. To further characterize the DCAF12 interactions with both MAGEA3 and CCT5, we developed a suite of biophysical and a proximity-based cellular NanoBRET assays showing that both MAGEA3 and CCT5 C-terminal degron peptides interact with DCAF12 in nanomolar affinity in vitro and in cells. Furthermore, we report here the 3.17 Å cryo-EM structure of DCAF12-DDB1-MAGEA3 complex revealing the key DCAF12 residues involved in C-terminal degron recognition and binding. Our study provides new tools and resources to enable the discovery of small molecule handles targeting the WDR domain of DCAF12 for future PROTAC design and development.

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Publisher

Cold Spring Harbor Laboratory

Subject

Biochemistry