Very excited to share this one! Our comprehensive structure, genetics and biophysics dissection of which flagellar dyneins and other proteins are needed for flagella to beat and drive cells swimming behaviours: www.biorxiv.org/content/10.1...
Mark your calendars! The CSHA Cilia & Centrosomes meeting returns this November 2025, can’t wait for what’s sure to be an exceptional gathering of the community.
*Deadline extended*
Applications for this year's #CryoEM Data Processing Workshop are due March 27!
Don't miss this chance to learn about various approaches to deal with conformational/compositional heterogeneity.
myumi.ch/lsi-cryo-2025
@jbquerido.bsky.social
@shyamalm.bsky.social
A reminder that the Brown lab has an opening for a postdoc fellow: brown.hms.harvard.edu/jobs/242. This might suit someone from the #cilia community interested in learning structural biology. Deadline extended to the 10th Jan.
Delighted to have contributed to this paper and amazing resource. In-silico protein-protein interaction screening has huge promise for generating novel hypotheses and building models into low-res #cryo-EM and #teamtomo maps.
Watching Sven elucidate this mechanism from an unbiased screen onwards has been one of my favorite experiences as a PI. In these challenging times for science at Harvard, it reminds me of the sheer joy of doing science and making discoveries.
The insides of microtubules of motile cilia and flagella are coated in proteins - but are they all important for motility? Our latest collaborative study addresses this question using trypanosomatids as model organisms. Matt explains more below:
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
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
Our latest collaborative effort - with Eva Gluenz and @zephyris-science.bsky.social - to understand how the various proteins and complexes of the axoneme contribute to ciliary motility:
Richard Wheeler
Alan Brown
Alan Brown
Alan Brown
U-M Life Sciences Institute
Paul & Virginie - Centriole Lab
Alan Brown
Alan Brown
Alan Brown
Alan Brown
The Brown lab at Harvard Medical School is seeking a highly motivated postdoctoral fellow to join our team.
Thrilled to share that the final piece of my PhD work is now on bioRxiv! biorxiv.org/content/10.1... With support from @nvidia and the @NSF, we used AlphaFold to screen 1.6M+ protein pairs, revealing thousands of potential novel PPIs. All data can be viewed at predictomes.org/hp
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
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?
I am super excited to share our latest work on the structures of doublet microtubules from trypanosomatid parasites, the causative agents of leishmaniasis, Chagas disease, and African sleeping sickness. tinyurl.com/48sh3xn5
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...
Protein-protein interactions (PPIs) drive virtually all biological processes, yet most PPIs have not been identified and even more remain structurally unresolved. We developed a two-step computational...
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
The movement and pathogenicity of trypanosomatid species, the causative agents of trypanosomiasis and leishmaniasis, are dependent on a flagellum that contains an axoneme of dynein-bound doublet micro...
