Rapoport Lab

Read our latest #research "The deubiquitinating enzyme Otu1 releases substrates from the conserved initiation complex of the Cdc48/p97 ATPase for proteasomal degradation" published in Sci Rep (2026). https://doi. org/10.1038/s41598-026-42811-6

Read our latest #research "A heterotrimeric protein complex assembles the metazoan V-ATPase upon dissipation of proton gradients", published with @SpringerNature in @NatureSMB nature.com/articles/s4159…

Read our latest #research "Import mechanism of peroxisomal proteins with an N-terminal signal sequence", published with @SpringerNature in @NatureCellBio rdcu.be/elkQ3

Excited to share our latest work led by our postdoc Dan Zhao! We uncovered how the bifunctional complex of Mnl1 mannosidase and protein disulfide isomerase (Pdi1) initiates ERAD. A long-sought ERAD reductase is finally discovered! #Sec11" target="_blank" rel="nofollow noopener">nature.com/articles/s4159… Huge congratulations!

@ninawowp @HHMINEWS science.org/doi/10.1126/sc…

@RapoportLab @HHMINEWS Link requires a Harvard login

Mystery unveiled! Peroxisomal protein import resembles that of nuclear pore! Congratulations to Yuan and Mike for their joint effort! Thanks to @HHMINEWS for their continuous support on this project! …science-org.ezp-prod1.hul.harvard.edu/doi/10.1126/sc…

We are thrilled to share our new work published in Nature today reporting a long-sought peroxisomal retrotranslocation channel formed by a ubiquitin ligase complex. Phenomenal work by our postdocs Peiqiang Feng, Xudong Wu and collaborators. nature.com/articles/s4158…

@ZhejianJ @jrengen @GygiLab

Our story on substrate translocation mechanism by Cdc48 is online now. Check out this Christmas present here authors.elsevier.com/c/1eIIX3vVUPGL…. Big thanks to everyone for their excellent contributions.

@Shenhav_Lab @ZhejianJ @jrengen @GygiLab We don't think the Cdc48 complex has any substrate specificity. According to our IP mass spec experiment performed in yeast lysate, most proteins with a K48-linked ubiquitin chain can bind the ATPase complex.

@RapoportLab @ZhejianJ @jrengen @GygiLab If the Cdc48 complex recognizes primarily polyubiquitin chains what confers substrate specificity?

Check out our new preprint on the translocation mechanism of the holy-grail Cdc48 ATPase. Congrats to @ZhejianJ and Hao Li, as well as to our wonderful collaborators the Engen lab @jrengen , the Marto lab, and @GygiLab !

Legobodies are online now, with full sequences available! Have fun!👉pnas.org/content/118/41…

@JiaweiZhao5 The sample with only the nanobody won't even survive till the grid preparation step-> heavy aggregates

@RapoportLab I am curious if KDELR-nanobody (not Legobody) will give a similar or better resolution map on Cryo-EM. Probably will 🤪

Check out our new preprint on Making the nanobody Big again for Cryo-EM, spearheaded by Xudong Wu (will start his own lab at Westlake University soon) in the lab.👉 biorxiv.org/content/10.110…

Excited to share our study on the mechanisms underlying selective autophagy of lipid droplets. We showed that Troyer syndrome protein spartin is a key to this! A wonderful collaboration with @synapsepark and @TalleyJLambert. Amazing support:@DamonRunyon biorxiv.org/content/10.110…

Check out our new review on protein translocation through a distorted lipid bilayer. authors.elsevier.com/c/1cVIr3QxxSjU…

@A_Amunts It is tricky, but we are working on solving the structure by cryo-EM.

Want to know what will happen if a membrane protein is too good at generating curvature? Check our new paper nature.com/articles/s4146…

@tweet Want to know what will happen if a membrane protein is too good at generating curvature? Check our new paper nature.com/articles/s4146…

#CryoEM structure of the post‐translational Sec #translocon with substrate bound and X-ray/HDX of the Sec62 subunit. ➡️ @embojournal paper online now! Congrats to @tw_weng, @jingdongcheng, @BangeBalcony and everyone involved! 🎉👏 embopress.org/doi/abs/10.152…