H. Walden

Structural and biochemical basis of FANCI-FANCD2 interdependent ubiquitination

This paper presents a cryo-EM structure of the FANCI-FANCD2 complex bound to DNA, showing how ubiquitination dynamics regulate its function in DNA repair.

Cryo-EM reveals a mechanism of USP1 inhibition through a cryptic binding site

The paper uses cryo-EM to reveal how ML323 inhibits USP1 by displacing part of its hydrophobic core, causing conformational changes that disrupt the active site.

Distinct phosphorylation signals drive acceptor versus self-ubiquitination selection by Parkin

This study shows parkin uses distinct phosphorylation signals for ubiquitinating acceptor proteins versus self-ubiquitination, with phosphorylation triggering autoubiquitination.

Structural basis of FANCD2 deubiquitination by USP1-UAF1

This study determines the structural basis of FANCD2 deubiquitination by USP1-UAF1, revealing conformational changes and substrate recognition mechanisms.

Differential functions of FANCI and FANCD2 ubiquitination stabilize ID2 complex on DNA

This study identifies how ubiquitination of FANCI and FANCD2 stabilizes the ID2 complex on DNA, enhancing its affinity for double-stranded DNA and protecting ubiquitin from deubiquitination.

Specificity for deubiquitination of monoubiquitinated FANCD2 is driven by the N-terminus of USP1

This study identifies the N-terminus of USP1 as critical for its specificity in deubiquitinating FANCD2, but not PCNA or FANCI.

Allosteric network in Ube2T drives specificity for RING E3 catalysed ubiquitin signals.

The paper identifies an allosteric network in Ube2T that enhances FANCD2 ubiquitination while maintaining specificity, and reveals similar networks in other E2s.

Synergistic Recruitment of UbcH7~Ub and Phosphorylated Ubl Domain Triggers Parkin Activation

This study reveals how phosphorylation and ubiquitin binding synergistically activate parkin by reorganizing its structure to facilitate ubiquitin transfer.