Sara Šepić
@sarasepic.bsky.social
PhD student in Schulman lab @mpibiochem.bsky.social Navigating through biochemistry and structural biology of ubiquitin world 👩🏼🔬 🔬
Excited to share our latest work on understanding CTLH-MKLN1 substrate recruitment. Stay tuned for the paper 🤗
bioRxiv Biochemistry@biorxiv-biochem.bsky.social · 4w agoMultimodal substrate recruitment enables CTLH-MKLN1 E3 ligase to target N-, C-, and internal degrons https://www.biorxiv.org/content/10.64898/2026.09.10.750665v1
Schulman lab is ready for the GRK2243 Symposium: Understanding ubiquitination: from molecular mechanisms to disease in würzburg #wUeBI2025 @grk2243.bsky.social @jakobfarnung.bsky.social @samuelmaiwald.bsky.social @hannahbkmpr.bsky.social
Excited to share our latest study on how K29/K48-branched #ubiquitin chains are forged by the #E3 ligase TRIP12, and how this suggests a consensus mechanism for chain formation by HECT E3s! @natsmb.nature.com 1/7 www.nature.com/articles/s41...
TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains - Nature Structural & Molecular Biology
Using biochemistry, chemical biology, and cryo-EM, Maiwald et al. elucidate how TRIP12 forms K29 linkages and K29/K48-linked branched ubiquitin chains, revealing a mechanism for polyubiquitylation sha...
nature.com