Working @adelmanlab.bsky.social @hms-bcmp.bsky.social + Vik Khurana lab @mgbresearch.bsky.social. Previously at Eilers/Wolf Lab @uni-wuerzburg.de. Interested in transcription and dsRNA biology - with a special focus on RNA Pol II.
Apoorva Baluapuri
Loading...
Excited to see this work published online at @cp-cell.bsky.social today!
www.cell.com/cell/fulltex...
CFAP36, a conserved cilia-specific ubiquitin reader, partners with the ARL3 GTPase
to enable the selective and directional retrieval of polyubiquitinated proteins from
cilia, a process essential for m...
Much appreciate the spotlight on our (@adelmanlab.bsky.social) paper about INT depletion/dsRNA-induced stress responses by @hanzlikovalab.bsky.social Amazing to see the finding being placed in perspective of the big picture of neurodevelopmental diseases and therapeutic targets 🙏 #RNABiology
Sven Lange
How do cells keep their cilia “clean” and functional? Our new study uncovers a conserved mechanism for retrieving polyubiquitinated proteins from #cilia – a process essential for cellular signaling and health. #cellbiology #ciliopathy #ubiquitin #IFT 🧵👇 1/n
Apoorva Baluapuri
The temporospatial distribution of proteins within cilia is regulated by intraflagellar transport (IFT), wherein molecular trains shuttle between the cell body and cilium. Defects in this process impair various signal-transduction pathways and cause ciliopathies. Although K63-linked ubiquitination appears to trigger protein export from cilia, the mechanisms coupling polyubiquitinated proteins to IFT remain unclear. Using a multidisciplinary approach, we demonstrate that a complex of CFAP36, a conserved ciliary protein of previously unknown function, and ARL3, a GTPase involved in ciliary import, binds polyubiquitinated proteins and links them to retrograde IFT trains. CFAP36 uses a coincidence detection mechanism to simultaneously bind two IFT subunits accessible only in retrograde trains. Depleting CFAP36 accumulates K63-linked ubiquitin in cilia and disrupts Hedgehog signaling, a pathway reliant on the retrieval of ubiquitinated receptors. These findings advance our understanding of ubiquitin-mediated protein transport and ciliary homeostasis, and demonstrate how structural changes in IFT trains achieve cargo selectivity. ### Competing Interest Statement The authors have declared no competing interest. Sara Elizabeth O'Brien Trust Postdoctoral Fellowship awarded through the Charles A. King Trust Postdoctoral Research Fellowship Program, , 8460873-01 Richard and Susan Smith Family Foundation, https://ror.org/05j95n956, National Institute of General Medical Sciences (NIGMS), , R01GM141109, R01GM143183
Exciting new work from Apoorva Baluapuri of the Adelman lab! @baluapuri.bsky.social
@adelmanlab.bsky.social
www.sciencedirect.com/science/arti...
The Vlaming lab is expanding! If you are or know a good prospective PhD student, excited about studying transcription, please (suggest them to) apply here: www.uu.nl/en/organisat...
My biased opinion: exciting topic, super nice colleagues, and great research environment in a lovely city.
🎉 Thrilled to share our new paper in @narjournal.bsky.social!
We uncover how the Hox TF Ultrabithorax controls alternative splicing to shape muscle patterning and homeotic identity 🧬 @igmm-montpel.bsky.social
🔗 doi.org/10.1093/nar/...
Our collaborative paper with the Arndt lab is out today: doi.org/10.1093/nar/... (originally bioRxiv: www.biorxiv.org/content/10.1...). Here we asked the question of how CHD1 localizes to chromatin.
In the June 12th issue of Cell, Baluapuri et al. report that loss of the Integrator (INT) complex triggers cellular stress by unleashing aberrant transcription, resulting in production of immunogenic double-stranded RNA. Dissecting early and late consequences of INT depletion, the study exemplifies how transcriptional dysregulation can culminate in profound physiological outcomes.
Abstract. The dual interaction of many transcription factors (TFs) with both DNA and RNA is an underexplored issue that could fundamentally reshape our und
Integrator (INT) is a metazoan-specific complex that targets promoter-proximally paused RNA polymerase II (RNAPII) for termination, preventing immatur…
www.sciencedirect.com
Thrilled to see my work with @adelmanlab.bsky.social on INT/dsRNA highlighted by @willgarland.bsky.social and @heick.bsky.social ! Thanks for beautifully capturing how nuclear RNA guardians prevent cellular chaos. The ripple effects of transcriptional dysregulation are indeed profound! #RNABiology
Abstract. The nucleosome remodeler Chd1 is required for the re-establishment of nucleosome positioning in the wake of transcription elongation by RNA Polym
Do you or someone you know have an exciting new chromatin/transcription story that you'll be ready to talk about in the Fall?
Then fill out or share this form to speak in the @fnucleosome.bsky.social seminar series! All models, organisms, and complexes welcome 🧬🧪🔬
Cell Chemical Biology
Hanneke Vlaming
Harvard Med BCMP
We wrote a review on Transposable Elements (TEs) and almost all aspects of TE silencing and their roles in biological processes & disease.
www.nature.com/articles/s41...
Integrator complex collapse: A mechanistic route to integrated stress response and disease
Julie Carnesecchi
Thrilled to see my postdoc work at Adelman Lab @hms-bcmp.bsky.social on Integrator(INT) now out @cp-cell.bsky.social. We found that INT deficiency allows immature+unlicensed RNAPII to precociously enter genes. This immature RNAPII can transcribe short genes but terminates prematurely in long genes:
