Mechanistically, UFMylation and ubiquitination compete for the same lysine on IFT88, forming a mutually exclusive modification switch that controls protein stability and ciliary integrity across tissues.
January 29, 2026 at 2:49 PM
Mechanistically, UFMylation and ubiquitination compete for the same lysine on IFT88, forming a mutually exclusive modification switch that controls protein stability and ciliary integrity across tissues.
While ubiquitination is a well-known regulator of protein stability, the roles of many ubiquitin-like modifiers remain unclear. Here, UFL1-mediated UFMylation emerges as a protective signal for the ciliary protein IFT88.
January 29, 2026 at 2:49 PM
While ubiquitination is a well-known regulator of protein stability, the roles of many ubiquitin-like modifiers remain unclear. Here, UFL1-mediated UFMylation emerges as a protective signal for the ciliary protein IFT88.
💡 Ciliary homeostasis turns out to depend on an unexpected tug-of-war between UFMylation and ubiquitination.
In a recent editorial in Cell Death & Differentiation,
@jnpruneda.bsky.social and I highlight new work from Wang et al. 🧵👇
In a recent editorial in Cell Death & Differentiation,
@jnpruneda.bsky.social and I highlight new work from Wang et al. 🧵👇
January 29, 2026 at 2:49 PM
💡 Ciliary homeostasis turns out to depend on an unexpected tug-of-war between UFMylation and ubiquitination.
In a recent editorial in Cell Death & Differentiation,
@jnpruneda.bsky.social and I highlight new work from Wang et al. 🧵👇
In a recent editorial in Cell Death & Differentiation,
@jnpruneda.bsky.social and I highlight new work from Wang et al. 🧵👇
ICYMI: New Online! The mechanistic basis and cellular functions of UFMylation
The mechanistic basis and cellular functions of UFMylation
Nature Reviews Molecular Cell Biology, Published online: 09 January 2026; doi:10.1038/s41580-025-00944-yUFMylation, a ubiquitin-like modification, regulates endoplasmic reticulum-associated ribosome quality control by conjugating UFM1 to the ribosomal subunit RPL26, preserving ribosome integrity under stress. This Review explores the structural basis of UFMylation and its emerging functional breadth, and it discusses putative UFMylation substrates.
dlvr.it
January 12, 2026 at 10:49 AM
ICYMI: New Online! The mechanistic basis and cellular functions of UFMylation
A very nice #review on #UFMylation from the giants of the field: The mechanistic basis and cellular functions of UFMylation www.nature.com/articles/s41...
Client Challenge
www.nature.com
January 11, 2026 at 2:09 PM
A very nice #review on #UFMylation from the giants of the field: The mechanistic basis and cellular functions of UFMylation www.nature.com/articles/s41...
The mechanistic basis and cellular functions of UFMylation
->Nature | More from Lil Dr Glen EcoChat at BigEarthData.ai
->Nature | More from Lil Dr Glen EcoChat at BigEarthData.ai
The mechanistic basis and cellular functions of UFMylation
Kerscher, O., Felberbaum, R. & Hochstrasser, M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell Dev. Biol. 22, 159–180 (2006). Cappadocia, L. & Lima, C. D. Ubiquitin-like protein conjugation: structures, chemistry, and mechanism. Chem. Rev. 118, 889–918...
www.nature.com
January 10, 2026 at 2:44 AM
The mechanistic basis and cellular functions of UFMylation
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Client Challenge
www.nature.com
January 9, 2026 at 6:02 PM
The mechanistic basis and cellular functions of UFMylation
www.nature.com/articles/s41...
www.nature.com/articles/s41...
New Online! The mechanistic basis and cellular functions of UFMylation
The mechanistic basis and cellular functions of UFMylation
Nature Reviews Molecular Cell Biology, Published online: 09 January 2026; doi:10.1038/s41580-025-00944-yUFMylation, a ubiquitin-like modification, regulates endoplasmic reticulum-associated ribosome quality control by conjugating UFM1 to the ribosomal subunit RPL26, preserving ribosome integrity under stress. This Review explores the structural basis of UFMylation and its emerging functional breadth, and it discusses putative UFMylation substrates.
dlvr.it
January 9, 2026 at 10:48 AM
New Online! The mechanistic basis and cellular functions of UFMylation
UFMylation of 14-3-3ϵ coordinates MAVS signaling complex assembly to promote antiviral innate immune induction https://www.biorxiv.org/content/10.1101/2025.10.21.683613v1
October 24, 2025 at 5:16 PM
UFMylation of 14-3-3ϵ coordinates MAVS signaling complex assembly to promote antiviral innate immune induction https://www.biorxiv.org/content/10.1101/2025.10.21.683613v1
UFMylation of 14-3-3ϵ coordinates MAVS signaling complex assembly to promote antiviral innate immune induction https://www.biorxiv.org/content/10.1101/2025.10.21.683613v1
October 24, 2025 at 5:16 PM
UFMylation of 14-3-3ϵ coordinates MAVS signaling complex assembly to promote antiviral innate immune induction https://www.biorxiv.org/content/10.1101/2025.10.21.683613v1
Cells rely on protein “quality control” to stay healthy.
New research in The FASEB Journal shows that a process called UFMylation helps protect cells from stress by keeping a key protein, BiP, in balance.
Learn more 👉 buff.ly/RVryJgs
#FASEBJournal #ScienceCommunication #CellHealth
New research in The FASEB Journal shows that a process called UFMylation helps protect cells from stress by keeping a key protein, BiP, in balance.
Learn more 👉 buff.ly/RVryJgs
#FASEBJournal #ScienceCommunication #CellHealth
A Protein Modification is Critical for Maintaining ER Homeostasis
Researchers discovered that UFMylation—a protein modification—helps maintain endoplasmic reticulum (ER) balance by regulating the stability of BiP, a key st
buff.ly
October 21, 2025 at 2:56 PM
Cells rely on protein “quality control” to stay healthy.
New research in The FASEB Journal shows that a process called UFMylation helps protect cells from stress by keeping a key protein, BiP, in balance.
Learn more 👉 buff.ly/RVryJgs
#FASEBJournal #ScienceCommunication #CellHealth
New research in The FASEB Journal shows that a process called UFMylation helps protect cells from stress by keeping a key protein, BiP, in balance.
Learn more 👉 buff.ly/RVryJgs
#FASEBJournal #ScienceCommunication #CellHealth
Now we are looking for in vitro evidence on MCM UFMylation💪
Xingzhi Xu, Shunichi Takeda and collaborators show that UFL1-dependent #UFMylation of MCM5 promotes CMG replicative helicase formation and replication fork progression
www.embopress.org/doi/full/10....
www.embopress.org/doi/full/10....
September 19, 2025 at 2:05 AM
Now we are looking for in vitro evidence on MCM UFMylation💪
Xingzhi Xu, Shunichi Takeda and collaborators show that UFL1-dependent #UFMylation of MCM5 promotes CMG replicative helicase formation and replication fork progression
www.embopress.org/doi/full/10....
www.embopress.org/doi/full/10....
September 15, 2025 at 8:54 AM
Xingzhi Xu, Shunichi Takeda and collaborators show that UFL1-dependent #UFMylation of MCM5 promotes CMG replicative helicase formation and replication fork progression
www.embopress.org/doi/full/10....
www.embopress.org/doi/full/10....
By developing an antibody-based method using mass spec, this study uncovered >200 UFMylation sites across mouse tissues—including on myosin. Myosin UFMylation is elevated in skeletal muscle from people with ALS, suggesting in vivo UFMylation is more dynamic than expected www.cell.com/cell-reports...
Site-specific quantification of the in vivo UFMylome reveals myosin modification in ALS
UFMylation is the post-translational modification of Ubiquitin Fold Modifier1 (UFM1)
applied to substrate proteins. Blazev et al. develop an antibody-based enrichment
approach followed by LC-MS/MS to ...
www.cell.com
August 6, 2025 at 8:04 PM
By developing an antibody-based method using mass spec, this study uncovered >200 UFMylation sites across mouse tissues—including on myosin. Myosin UFMylation is elevated in skeletal muscle from people with ALS, suggesting in vivo UFMylation is more dynamic than expected www.cell.com/cell-reports...
UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair https://www.biorxiv.org/content/10.1101/2025.06.16.659844v1
June 18, 2025 at 3:18 AM
UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair https://www.biorxiv.org/content/10.1101/2025.06.16.659844v1
UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair https://www.biorxiv.org/content/10.1101/2025.06.16.659844v1
June 18, 2025 at 3:18 AM
UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair https://www.biorxiv.org/content/10.1101/2025.06.16.659844v1
Highlight on our recent work on UFMylation by @dimitristypas.bsky.social on @NatureSMB: www.nature.com/articles/s41...
UFMylation-dependent quality control of ER-stalled ribosomes - Nature Structural & Molecular Biology
Nature Structural & Molecular Biology - UFMylation-dependent quality control of ER-stalled ribosomes
www.nature.com
June 15, 2025 at 7:06 PM
Highlight on our recent work on UFMylation by @dimitristypas.bsky.social on @NatureSMB: www.nature.com/articles/s41...
ICYMI: New online: UFMylation-dependent quality control of ER-stalled ribosomes
UFMylation-dependent quality control of ER-stalled ribosomes
Nature Structural & Molecular Biology, Published online: 12 June 2025; doi:10.1038/s41594-025-01606-5UFMylation-dependent quality control of ER-stalled ribosomes
go.nature.com
June 13, 2025 at 10:00 AM
ICYMI: New online: UFMylation-dependent quality control of ER-stalled ribosomes
A Review published in Molecular Neurodegeneration discusses the many connections between UFMylation with Alzheimer’s disease pathogenesis, emphasizing the role of UFMylation in these pathways and their abnormalities in AD.
bit.ly/4mUv03a
#MedSky #alzsky
bit.ly/4mUv03a
#MedSky #alzsky
June 12, 2025 at 4:30 PM
A Review published in Molecular Neurodegeneration discusses the many connections between UFMylation with Alzheimer’s disease pathogenesis, emphasizing the role of UFMylation in these pathways and their abnormalities in AD.
bit.ly/4mUv03a
#MedSky #alzsky
bit.ly/4mUv03a
#MedSky #alzsky
New online: UFMylation-dependent quality control of ER-stalled ribosomes
UFMylation-dependent quality control of ER-stalled ribosomes
Nature Structural & Molecular Biology, Published online: 12 June 2025; doi:10.1038/s41594-025-01606-5UFMylation-dependent quality control of ER-stalled ribosomes
go.nature.com
June 12, 2025 at 9:59 AM
New online: UFMylation-dependent quality control of ER-stalled ribosomes
Excited to share our new paper led by recent PhD, Dr. Hannah Schmidt! We found that UFMylation unexpectedly promotes flavivirus particle production by specifically regulating viral assembly. Check it out! #virology #UFMylation #flaviviruses
journals.asm.org/doi/10.1128/...
journals.asm.org/doi/10.1128/...
June 5, 2025 at 3:21 PM
Excited to share our new paper led by recent PhD, Dr. Hannah Schmidt! We found that UFMylation unexpectedly promotes flavivirus particle production by specifically regulating viral assembly. Check it out! #virology #UFMylation #flaviviruses
journals.asm.org/doi/10.1128/...
journals.asm.org/doi/10.1128/...
'The many connections of #UFMylation with #AlzheimersDisease: a comprehensive review'
Tingxiang Yan, Benjamin D. Clarkson, Zhenkun Lou, Wolfdieter Springer & Fabienne C. Fiesel @fabiennefiesel.bsky.social
molecularneurodegeneration.biomedcentral.com/articles/10....
Tingxiang Yan, Benjamin D. Clarkson, Zhenkun Lou, Wolfdieter Springer & Fabienne C. Fiesel @fabiennefiesel.bsky.social
molecularneurodegeneration.biomedcentral.com/articles/10....
The many connections of UFMylation with Alzheimer’s disease: a comprehensive review - Molecular Neurodegeneration
Alzheimer’s disease (AD) is a complex neurodegenerative disorder that is characterized by the accumulation of pathologic tau and beta-amyloid proteins. UFMylation is an emerging ubiquitin-like post-tr...
molecularneurodegeneration.biomedcentral.com
June 4, 2025 at 3:03 PM
'The many connections of #UFMylation with #AlzheimersDisease: a comprehensive review'
Tingxiang Yan, Benjamin D. Clarkson, Zhenkun Lou, Wolfdieter Springer & Fabienne C. Fiesel @fabiennefiesel.bsky.social
molecularneurodegeneration.biomedcentral.com/articles/10....
Tingxiang Yan, Benjamin D. Clarkson, Zhenkun Lou, Wolfdieter Springer & Fabienne C. Fiesel @fabiennefiesel.bsky.social
molecularneurodegeneration.biomedcentral.com/articles/10....
Loss of UFMylation supports prostate cancer metastasis and rewires cell metabolism towards hexosamine biosynthesis https://www.biorxiv.org/content/10.1101/2025.06.02.657324v1
June 4, 2025 at 1:48 PM
Loss of UFMylation supports prostate cancer metastasis and rewires cell metabolism towards hexosamine biosynthesis https://www.biorxiv.org/content/10.1101/2025.06.02.657324v1
Loss of UFMylation supports prostate cancer metastasis and rewires cell metabolism towards hexosamine biosynthesis https://www.biorxiv.org/content/10.1101/2025.06.02.657324v1
June 4, 2025 at 1:48 PM
Loss of UFMylation supports prostate cancer metastasis and rewires cell metabolism towards hexosamine biosynthesis https://www.biorxiv.org/content/10.1101/2025.06.02.657324v1
UFMylation promotes orthoflavivirus infectious particle production journals.asm.org/doi/10.1128/...
UFMylation promotes orthoflavivirus infectious particle production | Journal of Virology
Orthoflaviviruses depend on host-mediated post-translational modifications to successfully
complete their life cycle, yet many of these critical interactions remain undefined.
Here, we describe a role...
journals.asm.org
June 3, 2025 at 3:03 PM
UFMylation promotes orthoflavivirus infectious particle production journals.asm.org/doi/10.1128/...