A human-specific regulatory mechanism revealed in a pre-implantation model Nature - Genetic manipulation of blastoids reveals the role of recently emerged transposable elements and genes in human development.

Today in @nature.com, we present our work leveraging functional genomics and human blastoids to uncover a human-specific mechanism in preimplantation development driven by the endogenous retrovirus HERVK.
Special thanks to the reviewers whose comments improved our manuscript a lot! rdcu.be/eI3tD

Fantastic work Raquel! So well deserved

Behind the Science: How a ‘speech gene’ could help treat Huntington’s Stanford Medicine researchers found cells that keep a speech-linked protein called FOXP2 from clumping; its tricks could break apart clumps of proteins that cause devastating brain diseases.

I’m very excited to share that Stanford Medicine has highlighted my work

med.stanford.edu/news/insight...

Excited to share Benson’s and Maria’s work in collab w/Kostas Tzelepis: we found the nucleolar protein NPM1 is a marker of AML and can be targeted therapeutically

connecting ‘cell surface RNA biology’ to cancer biology

@natbiotech.nature.com
www.nature.com/articles/s41...

DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-p...

What did the two amino acid substitutions in #FOXP2 that occurred uniquely in the human lineage do? 🧪🧬 🧠
Fascinating new @cp-cell.bsky.social study by @shadys11.bsky.social D. Jarosz & J. Wysocka, uncovering a molecular function for these 2 substitutions in promoting the solubility of FOXP2. (1/n)

DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-p...

When we first isolated FOXP2 & implicated it in speech disorder, a notable feature was its big stretch of consecutive glutamine (Q) residues, the longest polyQ tract in a native protein. @shadys11.bsky.social et al here use it as a model to reveal how polyQ proteins avoid forming toxic assemblies.🙌🧪

Functional dissection of two amino acid substitutions unique to the human FOXP2 protein - Scientific Reports Scientific Reports - Functional dissection of two amino acid substitutions unique to the human FOXP2 protein

To our surprise, there is more contribution for the N303 site on the solubility of FOXP2.
The same site is also contributing more to certain humanized mouse phenotypes

www.nature.com/articles/s41...

Thank you!

Thank you Christa!!

DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-p...

I am incredibly proud to share that my work has officially been published in Cell! @cp-cell.bsky.social
This work was a product of years of dedication and countless hours of research in the labs of Joanna Wysocka and Dan Jarosz labs @stanfordmedicine.bsky.social

www.cell.com/cell/fulltex...

DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-promoting mechanisms utilized by FOXP2 diminishes aggregation and amyloid formation by the pathological form of Huntingtin polyQ.

Now online! DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation