Kashish Singh

@kashishsingh.bsky.social

Postdoc @Carter_Lab @MRC_LMB. Alumnus of the Stark lab @mpi_nat.

How are mRNAs linked to molecular motors in mammalian cells? In our new preprint, we show that FXR1/2 are RNA adaptors for the microtubule motor dynein. Our findings have also prompted us to rethink how activating adaptors contribute to motor-based transport (1/n)

bioRxiv Cell Biology@biorxiv-cellbio.bsky.social · 2w ago

FXR proteins and BICD2 cooperate to promote dynein-mediated RNP transport and stress granule assembly https://www.biorxiv.org/content/10.64898/2026.09.25.754448v1

Very happy to see the final version of our work on the structure and composition of cytoplasmic lattices in mouse embryos, previously shared on bioRxiv, now published in The EMBO Journal! Many thanks to our editor, Ieva Gailite, and the reviewers for their constructive input.

The EMBO Journal@embojournal.org · 2mo ago

What’s the function of embryonic ‘cytoplasmic lattices’? Using cryo-ET, @kashishsingh.bsky.social @carter-lab.bsky.social and coworkers reveal them as megadalton-size hubs of ubiquitination proteins/ubiquitin transfer link.springer.com/article/10.1...

Disrupting phage liquid crystalline droplets restores antibiotic susceptibility in Pseudomonas aeruginosa biofilms out in @plosbiology.org by @abultarafder.bsky.social and team. Exciting collaboration with @geiselbiofilm.bsky.social @pearce-maths.bsky.social and others

PLOS Biology@plosbiology.org · 4mo ago

#Biofilm matrices containing filamentous phages help #Pseudomonas aeruginosa tolerate antibiotics. @abultarafder.bsky.social @tbharat-lab.bsky.social &co show that #nanobody disruption of #phage Pf4 #LiquidCrystalline droplets restores #antibiotic susceptibility @plosbiology.org 🧪 plos.io/4xkd6Mw

Top: Nanobody binders are potent inhibitors of Pf4 liquid crystalline droplet formation and disrupt preformed droplets. Cryo-ET of Pf4 liquid crystalline droplets incubated with Nb43. Tomographic slice of a Pf4 liquid crystalline droplet specimen incubated with (left) 0.1 μM and (right) 1 μM Nb43. Bottom: Schematic representation of nanobody action in abolishing antibiotic tolerance of P. aeruginosa biofilms. In untreated biofilms (left), cells show increased antibiotic tolerance due to Pf4 liquid crystalline droplets formed by depletion attraction in the biofilm EPS matrix, where encapsulated cells are protected by an antibiotic diffusion block. In nanobody treated biofilms, patchy binding of nanobody to Pf4 filaments reduces depletion attraction between the filaments preventing liquid crystalline droplet formation and encapsulation of cells, leading to increased antibiotic susceptibility of bacteria within the biofilm.

How do sperm and egg fuse? Surprisingly, we still don’t fully know… Our field has uncovered many pieces of the fertilization puzzle, but not how they fit together. We identify ✨ SPARK ✨ - a conserved sperm complex that couples sperm-egg binding to fusion. tinyurl.com/34cm4xat Read on! 🧵👇

Really exciting to see our new review published! This review explores the evolutionary history of the extra-embryonic endoderm, an evolutionarily ancient tissue co-opted to form the yolk sac, and explores how in vitro models are uncovering its biology. Check it out here: doi.org/10.1242/dev....

The vertebrate yolk sac: evolutionary origins and current advances in in vitro models

Summary: This Review examines the evolutionary history of the extra-embryonic endoderm, an evolutionarily ancient tissue co-opted to form the yolk sac, and explores how in vitro models are uncovering ...

doi.org

The #ADFLIP approach by @kaiyi94.bsky.social and @kjamali.bsky.social, combined with their approach to backpropagation through #AlphaFold2, is really powerful. Keep tuned for more exciting results! 🥳

Kai Yi@kaiyi94.bsky.social · 6mo ago

Thrilled with the our results with @kjamali.bsky.social and @sjorsscheres.bsky.social from the recent binder competition! 🎉 2 of our 7 designs successfully bound to the target, with affinities ranking 2nd and 3rd overall. All of these designs targeted the disordered region of the protein.