A new paper reports the structure of the E4 enzyme Ufd2, which mediates K48 branched ubiquitination on K29diUb and K29triUb, identifying Ufd2’s core region as a K29diUb binding domain and a dimeric conformation for distal ubiquitin stabilization www.nature.com/articles/s41...

Super excited to share our new #preprint on #BioRxiv ✨ We reveal the structural basis of a partnership between the ER membrane complex (EMC) and the P5A-ATPase Spf1 — an insertase–dislocase duo that coordinates membrane protein biogenesis and quality control. www.biorxiv.org/content/10.1...

Excited to share our latest study in @natcomms.nature.com , where we characterize the chaperone function of the ER membrane protein complex (EMC)—supporting membrane protein biogenesis beyond insertion! 1/9 www.nature.com/articles/s41...

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

Check out our latest study @natsmb.nature.com‬: Establishing a consensus model for #ubiquitin chain assembly by HECT #E3 ligases: #cryoEM structures of #TRIP12 forming K29-linked and K29/K48-branched chains! ❕ www.nature.com/articles/s41... @samuelmaiwald.bsky.social @unileiden.bsky.social

New online: TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains

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...

Super excited to share our latest work on deciphering the #Ubiquitin Code “𝗨𝗯𝗶𝗥𝗘𝗔𝗗 𝗱𝗲𝗰𝗶𝗽𝗵𝗲𝗿𝘀 𝗽𝗿𝗼𝘁𝗲𝗮𝘀𝗼𝗺𝗮𝗹 𝗱𝗲𝗴𝗿𝗮𝗱𝗮𝘁𝗶𝗼𝗻 𝗰𝗼𝗱𝗲 𝗼𝗳 𝗵𝗼𝗺𝗼𝘁𝘆𝗽𝗶𝗰 𝗮𝗻𝗱 𝗯𝗿𝗮𝗻𝗰𝗵𝗲𝗱 𝗞48 𝗮𝗻𝗱 𝗞63 𝘂𝗯𝗶𝗾𝘂𝗶𝘁𝗶𝗻 𝗰𝗵𝗮𝗶𝗻𝘀” @cp-molcell.bsky.social 1/8 www.cell.com/molecular-ce...