Samuel Maiwald
@samuelmaiwald.bsky.social
BIF PhD student in Schulman lab @mpibiochem.bsky.social, interested in structural biology and ubiquitin system
Comparison to our previous structure showing K48 chain formation by UBR5 suggests a consensus architecture for linkage-specific chain formation by HECT E3s.
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May 26, 2025 at 9:37 AM
Comparison to our previous structure showing K48 chain formation by UBR5 suggests a consensus architecture for linkage-specific chain formation by HECT E3s.
6/7
6/7
On the other side, acceptor and donor ubiquitins come together with the TRIP12 HECT domain to establish the active site. Both sides cooperate to precisely place K29 of the proximal acceptor ubiquitin for catalysis.
5/7
5/7
May 26, 2025 at 9:37 AM
On the other side, acceptor and donor ubiquitins come together with the TRIP12 HECT domain to establish the active site. Both sides cooperate to precisely place K29 of the proximal acceptor ubiquitin for catalysis.
5/7
5/7
One TRIP12 side avidly recruits the K48-linked chain, explaining preference for the proximal ubiquitin.
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4/7
May 26, 2025 at 9:37 AM
One TRIP12 side avidly recruits the K48-linked chain, explaining preference for the proximal ubiquitin.
4/7
4/7
We used activity-based probes to trap TRIP12 in the act of forming a K29/K48-branched triUb and a K29-linked diUb. Visualizing these complexes using cryo-EM revealed TRIP12s catalytic mechanism.
3/7
3/7
May 26, 2025 at 9:37 AM
We used activity-based probes to trap TRIP12 in the act of forming a K29/K48-branched triUb and a K29-linked diUb. Visualizing these complexes using cryo-EM revealed TRIP12s catalytic mechanism.
3/7
3/7
TRIP12 adds K29-linked ubiquitin onto K48-linked ubiquitin chains. We show that TRIP12 preferentially modifies the proximal ubiquitin to form branched chains.
2/7
2/7
May 26, 2025 at 9:37 AM
TRIP12 adds K29-linked ubiquitin onto K48-linked ubiquitin chains. We show that TRIP12 preferentially modifies the proximal ubiquitin to form branched chains.
2/7
2/7
Comparison to our previous structure showing K48 chain formation by UBR5 suggests a consensus architecture for linkage-specific chain formation by HECT E3s.
6/7
6/7
May 26, 2025 at 9:25 AM
Comparison to our previous structure showing K48 chain formation by UBR5 suggests a consensus architecture for linkage-specific chain formation by HECT E3s.
6/7
6/7
On the other side, acceptor and donor ubiquitins come together with the TRIP12 HECT domain to establish the active site. Both sides cooperate to precisely place K29 of the proximal acceptor ubiquitin for catalysis.
5/7
5/7
May 26, 2025 at 9:21 AM
On the other side, acceptor and donor ubiquitins come together with the TRIP12 HECT domain to establish the active site. Both sides cooperate to precisely place K29 of the proximal acceptor ubiquitin for catalysis.
5/7
5/7
One TRIP12 side avidly recruits the K48-linked chain, explaining preference for the proximal ubiquitin.
4/7
4/7
May 26, 2025 at 9:21 AM
One TRIP12 side avidly recruits the K48-linked chain, explaining preference for the proximal ubiquitin.
4/7
4/7
We used activity-based probes to trap TRIP12 in the act of forming a K29/K48-branched triUb and a K29-linked diUb. Visualizing these complexes using cryo-EM revealed TRIP12s catalytic mechanism.
3/7
3/7
May 26, 2025 at 9:21 AM
We used activity-based probes to trap TRIP12 in the act of forming a K29/K48-branched triUb and a K29-linked diUb. Visualizing these complexes using cryo-EM revealed TRIP12s catalytic mechanism.
3/7
3/7
TRIP12 adds K29-linked ubiquitin onto K48-linked ubiquitin chains. We show that TRIP12 preferentially modifies the proximal ubiquitin to form branched chains.
2/7
2/7
May 26, 2025 at 9:21 AM
TRIP12 adds K29-linked ubiquitin onto K48-linked ubiquitin chains. We show that TRIP12 preferentially modifies the proximal ubiquitin to form branched chains.
2/7
2/7