Structural Biochemist. Postdoc in Brown lab @ Harvard Med🇺🇸 with interest in ubiquitin. Formerly MRC PPU🇬🇧🏴 MPI Dortmund🇩🇪 Ruhr-Uni Bochum🇩🇪. He/Him.
Sven Lange
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Our lab is seeking a Postdoctoral Fellow. The position is intentionally broad, as we are looking for outstanding researchers from diverse scientific backgrounds to advance our understanding of cilia and ciliopathies: academicpositions.harvard.edu/postings/15526
Excited to see this work published online at @cp-cell.bsky.social today!
www.cell.com/cell/fulltex...
academicpositions.harvard.edu
We invite applicants for a postdoctoral fellow position in the Brown lab at Harvard Medical School in Boston, Massachusetts. The Brown lab uses structural, biophysical, and biochemical approaches to d...
One, perhaps two, of our postdocs are moving on to faculty positions this year (more news soon!). While they're truly irreplaceable, it does mean that we have openings for new members to join our team studying #cilia. If interested, please apply: academicpositions.harvard.edu/postings/15526
50 day free access with this link ==> urldefense.proofpoint.com/v2/url?u=htt...
In an eight-person rowing boat, each rower contributes to movement but also has a unique role: balancing, powering, or setting the rhythm and pace. In our latest collaborative work we asked – do the eight dynein “rowers” in #cilia and #flagella operate in the same way?
Passionate about ubiquitin biology, its mechanistic underpinnings and therapeutic exploitation? We are looking for a PhD student or postdoc to join our team. Applications and informal inquiries welcome!
www.mpinat.mpg.de/19-26?c=3895...
Registration now open! 2026 #EMBO #Ubiquitin Workshop set in stunning Monopoli, Puglia 🇮🇹
Cutting edge science, great speakers, short talk opportunities, travel awards
Limited spaces. Dont miss out - register early!
Registration & more info: meetings.embo.org/event/26-ubi...
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...
www.cell.com
Excited to share that my 2025 collection of science-inspired drawings is now live on the Protein Data Bank (PDB) website. Thank you @rcsbpdb.bsky.social!
It is free to explore and download. I’d love to hear what you think!
pdb101.rcsb.org/sci-art/bezs...
Sven Lange
Alan Brown
The research group Ubiquitin Signaling Specificity (Dr. Sonja Lorenz) invites applications for the position as
PhD student or Postdoc (f/m/d)
– Understanding and manipulating ubiquitin ligase specifi...
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
Alan Brown
PDB-101: Training, Outreach, and Education portal of RCSB PDB
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
Excited to see this work published online at @cp-cell.bsky.social today!
www.cell.com/cell/fulltex...
Sven Lange
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...
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
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
