Just in time for #HumpDay : Our study Targeting DCAF5 suppresses #SMARCB1 -mutant #cancer via stabilizing SWI/SNF is online now in nature. Congratulations 🎉 to co-first authors Sandi-Radko-Juettner and Hong Yue and all co-authors on this story! 1/
nature.com/articles/s4158…

Grateful to St. Jude Research for this #pressrelease covering our latest work on DCAF5 in collaboration with Fischer Lab

Check out this stunning work led by Sandi and Hong Yue now out in nature uncovering the role of DCAF5 in cancer! Gorgeous mechanistic dTAG data, including validation in mice. Honored to be part of this amazing collaborative team. Congrats, all!! 🧵👇

Together with the Cravatt group, we have a new manuscript out reporting the chemoproteomic discovery of covalent FOXA1 ligands that bind its DNA-binding domain, corrupt its motif preferences, and redistribute it on the genome. 1/11 biorxiv.org/content/10.110…

Excited to share E3-substrate tagging by ubiquitin biotinylation (E-STUB) Nature Chemical Biology! E-STUB enables CUL-RING ligase substrate identification and may transform the way we study glues and PROTACs by directly studying substrate ubiquitylation. 1/
rdcu.be/dBZKx

A new study from Bullman and CJohnstonLab Fred Hutchinson Cancer Center out today nature. We identify a 'high-risk' clade of F. nucleatum that dominates the human CRC niche. Huge congrats to the amazing first author Dr. Martha Zepeda Rivera 🇲🇽 (she/her) and the incredible team.
🧵 from Chris 👇
nature.com/articles/s4158…

Our paper on functional discovery of protein degradation and stabilization effectors with proteome-scale induced proximity screens is out in its final version! 1/ nature.com/articles/s4158… rdcu.be/dBUju

Killer use of dTAG to study the fast biology of PP2A. Numerous new substrates annotated.

Thrilled to share that our manuscript exploring the substrate landscape of PPP2CA, the principle catalytic subunit of PP2A, is now published! If you're interested in whether your favourite protein might be a PP2A substrate, check it out! ⬇️

doi.org/10.1016/j.isci…

(5/14) Since ZNF143-mAID2 depletion is only ~95%, we thought remaining ZNF143 might be enough.

We then made clone D (ZNF143-dTAG), which results in complete depletion, and did deep Micro-C again.

Again, dZNF143 has no effect on loops, even ZNF143-bound loops, nor on insulation.

(1/14) Excited to share our new work on ZNF143/ZFP143 by Domenic Narducci

ZNF143 has been widely reported to be a general loop factor

Instead we and deWitLab in a companion preprint show that ZNF143 is a TF with no loop function:
biorxiv.org/content/10.110…
biorxiv.org/content/10.110…

Thomas Hunt Morgan David R. Liu Eric Fischer Thanks, all. That reads more like an insertional mutagenesis limitation than a degron tagging limitation. Works fine by MHEJ. Good question about off targets. Always possible but generally no. Here, from our index ms in nature. Irrespective bravo, a fine paper that contributes…

I love this paper from David R. Liu and Eric Fischer, and further optimized ZnF tags are warmly welcome. Question for you two: in the abstract you speak to “problems with current degron tags”. Are there problems with dTAG? Seems fully orthogonal, small, insertable, works in vivo,…

I am honored to join this incredible team with Chris Kemp, Elizabeth Swisher, and Steve Henikoff! Many thanks to the National Cancer Institute for the support. We are excited to degrade key cancer drivers!

Excellent review by Saurav Kumar and Behnam Nabet highlighting recent innovative approaches for chemically controlled protein relocalization. Thanks for also mentioning our self-localizing ligand approach!

Excellent new review from Behnam Nabet and Saurav Kumar surveying the emerging field of targeted protein relocalization. Much more work to do here!

Thanks Behnam Nabet and Saurav Kumar for highlighting this exciting field and the work of Christine Isadora Ng! Stay tuned for more soon!

The final 'VOR' for our aspartate sensor manuscript has now been published after peer review eLife - the journal. Updates include additional sensor characterization and demonstration of response to aspartate restoration in cells. Thanks to the editors and reviewers!
doi.org/10.7554/eLife.…