#Nup107
First OMERO.figure of #TiM2025 🤩 All credits to @nfdi4bioimage.bsky.social Data Steward Cornelia Wetzker of @tudresden.bsky.social

See omero.tim2025.de/figure/file/... if you'd like to play with the data yourself in #OMERO
March 19, 2025 at 8:16 AM
Thought I would make my bsky debut with one of my favourite NEBD movies

White: NDC80-EGFP (kinetochores)
Magenta: TMR::HALO-NUP107 (nuclear pores)

RPE-1 cell entering mitosis on the lattice light-sheet, caught automatically by CelFDrive.

#Microscopy #CellBiology #Mitosis #Science
August 28, 2026 at 7:09 PM
New work from the lab! C9orf72 ALS‐causing mutations lead to mislocalization and aggregation of nucleoporin Nup107 into stress granules - Bilican - FEBS Letters - Wiley Online Library febs.onlinelibrary.wiley.com/doi/10.1002/...
FEBS Press
Mutations in the C9orf72 gene represent the most common genetic cause of amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease. Using patient-derived neurons and C. elegans models, w...
febs.onlinelibrary.wiley.com
September 2, 2025 at 7:11 AM
Latest paper from my lab. Great collaboration with Marisa Otegui, Martin Parniske, and Haruko Imaizumi-Anraku. @manishbiotechie.bsky.social and Audrey Kalil demonstrated amazing perseverance.

NUP107-160 nuclear pore sub-complex members determine symbiotic ion channel localization in legumes
NUP107-160 nuclear pore sub-complex members determine symbiotic ion channel localization in legumes
The nuclear pore complex controls the movement of proteins into and out of the nucleus, allowing cells to regulate protein localization and abundance. This process influences how organisms respond to environmental stimuli. Components of the nuclear pore complex, including the NUP107-160 sub-complex, NUP133, NUP85, and NENA, are required for root nodulation and arbuscular mycorrhization in Lotus japonicus. However, the specific role of these nucleoporins in symbiotic signaling was poorly understood. Through reverse genetics, we discovered that NUP133 is also required for symbiosis in Medicago truncatula, although the mutant phenotypes were less pronounced than in Lotus. Overexpression of the symbiotic ion channels Medicago DMI1 and Lotus Castor and Pollux in the Lotus Ljnup133, Ljnup85, and Ljnena mutants partially alleviated the nodulation defects. Notably, in NUP107-160 sub-complex mutants of Lotus and Medicago, the accumulation of GFP-labeled Pollux and DMI1 on the inner nuclear membrane was reduced, indicating the NUP107-160 sub-complex plays a key role in regulating the distribution of DMI1 and Pollux on the nuclear envelope. This highlights the extreme sensitivity of nodulation in Lotus to changes in the abundance of Pollux on the inner nuclear membrane. In contrast, Medicago appears to exhibit greater tolerance to alterations in the distribution of DMI1 on the nuclear envelope.
sco.lt
June 24, 2026 at 6:55 PM
Nup107 is a crucial regulator of torso-mediated metamorphic transition in Drosophila melanogaster
#Drosophila
Nup107 is a crucial regulator of torso-mediated metamorphic transition in Drosophila melanogaster #Drosophila
PubMed link
pubmed.ncbi.nlm.nih.gov
March 11, 2026 at 3:23 AM
Nup107 is a crucial regulator of torso-mediated metamorphic transition in <i>Drosophila melanogaster</i>
Nup107 is a crucial regulator of torso-mediated metamorphic transition in Drosophila melanogaster
Y-complex nucleoporin, Nup107, can regulate ecdysone production by affecting the transcription of Halloween genes and levels of RTK receptor, torso, for the metamorphic transition from larva to pupa.
buff.ly
March 18, 2026 at 6:01 AM
For years, nucleoporins of the NUP107-160 complex were known to be essential for legume symbiosis, but the underlying mechanism remained unclear.

Our work shows that NUP133, NUP85, and NENA regulate the localization of key symbiotic ion channels (DMI1/Pollux) to the inner nuclear membrane.
Latest paper from my lab. Great collaboration with Marisa Otegui, Martin Parniske, and Haruko Imaizumi-Anraku. @manishbiotechie.bsky.social and Audrey Kalil demonstrated amazing perseverance.

NUP107-160 nuclear pore sub-complex members determine symbiotic ion channel localization in legumes
NUP107-160 nuclear pore sub-complex members determine symbiotic ion channel localization in legumes
The nuclear pore complex controls the movement of proteins into and out of the nucleus, allowing cells to regulate protein localization and abundance. This process influences how organisms respond to environmental stimuli. Components of the nuclear pore complex, including the NUP107-160 sub-complex, NUP133, NUP85, and NENA, are required for root nodulation and arbuscular mycorrhization in Lotus japonicus. However, the specific role of these nucleoporins in symbiotic signaling was poorly understood. Through reverse genetics, we discovered that NUP133 is also required for symbiosis in Medicago truncatula, although the mutant phenotypes were less pronounced than in Lotus. Overexpression of the symbiotic ion channels Medicago DMI1 and Lotus Castor and Pollux in the Lotus Ljnup133, Ljnup85, and Ljnena mutants partially alleviated the nodulation defects. Notably, in NUP107-160 sub-complex mutants of Lotus and Medicago, the accumulation of GFP-labeled Pollux and DMI1 on the inner nuclear membrane was reduced, indicating the NUP107-160 sub-complex plays a key role in regulating the distribution of DMI1 and Pollux on the nuclear envelope. This highlights the extreme sensitivity of nodulation in Lotus to changes in the abundance of Pollux on the inner nuclear membrane. In contrast, Medicago appears to exhibit greater tolerance to alterations in the distribution of DMI1 on the nuclear envelope.
sco.lt
June 24, 2026 at 9:49 PM
For #FluorescenceFirday, here are 2 still images from a z-stack movie of a live drosophila egg chamber stained with SPY555-tubulin and expressing Nup107-GFP. The movie was found in the recent article "Scaling behaviour and control of nuclear wrinkling" in Nature Physics.

doi.org/10.1038/s415...
.
September 22, 2023 at 7:13 AM
C9orf72 ALS-causing mutations lead to nucleoporin Nup107 aggregation and subsequent pathological changes https://www.biorxiv.org/content/10.1101/2025.04.16.649118v1
April 17, 2025 at 8:30 PM
🍂 Our November issue is here!

🧬 Editor's Choice: C9orf72-#ALS mutations lead to Nup107 aggregation
👩‍🔬 Scientists' Forum Presenting the winner of our #WomenInScience writing contest

Find the whole issue, featuring research articles on #neuroscience and #cancer, here:

➡️ bit.ly/3JGZG9q
November 10, 2025 at 7:11 PM
🚨Exciting news: A recent study from our #FOR5762 member @thevilchezlab.bsky.social has been selected for the cover of @febsletters.bsky.social!

Huge congrats to @thevilchezlab.bsky.social, Saygın Bilican and all co-authors for this fantastic highlight on #ALS-linked #Nup107 mislocalization! 🎉
November 11, 2025 at 8:00 AM
🚨Check out this brand new publication from the lab of our CRC 1678 project leader @thevilchezlab.bsky.social about how C9orf72 ALS‐causing mutations lead to mislocalization and aggregation of nucleoporin Nup107 into stress granules! Congrationlations to this achievement!🥳
September 2, 2025 at 2:20 PM
Read the #OpenAccess Research Article "Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427" here:
journals.biologists.com/dev/article/...
Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427
Highlighted Article: This study explains the role of Nup107 in maternal-to-zygotic transition through primary miR427 nuclear export.
journals.biologists.com
February 5, 2025 at 4:34 PM
Read the #OpenAccess Research Article "Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427" here:
https://journals.biologists.com/dev/article/152/2/dev202865/365498/Nup107-contributes-to-the-maternal-to-zygotic
journals.biologists.com
February 5, 2025 at 4:29 PM
C9orf72 ALS-causing mutations lead to nucleoporin Nup107 aggregation and subsequent pathological changes https://www.biorxiv.org/content/10.1101/2025.04.16.649118v1
April 17, 2025 at 8:30 PM
Nuclear ex-pore-ation

Read this Research Highlight showcasing work from Valentyna Kostiuk, Mustafa Khokha @yaleschoolofmed.bsky.social and colleagues:
journals.biologists.com/dev/article/...
February 5, 2025 at 4:34 PM
Nice commentary on our paper! -> Putting channels in their place: nucleoporins and symbiotic signaling in legumes
Putting channels in their place: nucleoporins and symbiotic signaling in legumes
Every cell must decide what enters the nucleus and what stays out. The nuclear pore complex (NPC), built from proteins called nucleoporins (NUPs), spans the double membrane of the nuclear envelope and shuttles molecules between the cytoplasm and the nucleus. Most NPC components serve this universal housekeeping role, so it was striking when a handful turned out to matter specifically for symbiosis. The NUP107-160 subcomplex, which forms the outer ring of the pore (Tamura et al. 2010), was first linked to symbiosis in the model legume Lotus japonicus. Mutants in 3 of its members, NUP133, NUP85, and NENA, show impaired root nodulation and arbuscular mycorrhization. These mutants also lack the nuclear calcium spiking triggered by host perception of symbiotic microbes (Kanamori et al. 2006; Saito et al. 2007; Groth et al. 2010). This calcium spiking requires nuclear envelope-localized cation channels, CASTOR and POLLUX, in Lotus (Charpentier et al. 2008). The same pathway operates in the related model legume Medicago truncatula, where the Pollux ortholog DMI1 fills this role (Ané et al. 2004). The function of these channels likely depends on reaching the inner nuclear membrane, but how these NUPs influence symbiotic signaling has remained unclear for nearly 2 decades.
sco.lt
August 31, 2026 at 11:52 PM
RRIDs were included in this in eLife paper. We value the author's support of reproducibility. #OpenScience #ReproducibleResearch #BetterScience
Nup107 is a crucial regulator of torso-mediated metamorphic transition in Drosophila melanogaster
Y-complex nucleoporin, Nup107, can regulate ecdysone production by affecting the transcription of Halloween genes and levels of RTK receptor, torso, for the metamorphic transition from larva to pupa.
doi.org
March 19, 2026 at 7:05 AM
The authors included RRIDs in their None paper! RRIDs improve reproducibility in scientific research. #ReproducibleResearch #accelerateopenscience #RRID
C9orf72 ALS-causing mutations lead to mislocalization and aggregation of nucleoporin Nup107 into stress granules
doi.org
September 13, 2025 at 7:00 AM
Authors published a paper in Biorxiv, they used ImageJ in the study. Including #RRIDs will make this less ambiguous.

SciScore made a table with this resource, see “Automated Services” module (download as csv, xml or #jats) #STMpublishing #reproducibility
C9orf72 ALS-causing mutations lead to nucleoporin Nup107 aggregation and subsequent pathological changes
www.biorxiv.org
April 21, 2025 at 12:01 PM
3/ In healthy breast, 46% of long-read eIsoforms were unique despite 93.7% being present in GENCODE. The problem is read dilution across irrelevant isoforms, not transcript absence. At MARK1 and NUP107, long-read annotations recovered regulatory signals entirely missed by GENCODE.
March 24, 2026 at 6:43 PM
Nuclear ex-pore-ation

Read this Research Highlight showcasing work from Valentyna Kostiuk, Mustafa Khokha @yaleschoolofmed.bsky.social and colleagues:
https://journals.biologists.com/dev/article/152/2/e152_e0203/365514/Nuclear-ex-pore-ation
February 5, 2025 at 4:29 PM
The plot thickens! The fission yeast NPC may have asymmetric Y-complexes in its outer rings (https://www.biorxiv.org/content/early/2018/10/24/223131), just like the Chlamy NPC (https://www.nature.com/articles/s41467-018-04739-y). Meanwhile budding yeast and humans have symmetric...
Asymmetrical localization of Nup107-160 subcomplex compon...
The nuclear pore complex (NPC) forms a gateway for nucleo...
www.biorxiv.org
November 23, 2024 at 1:30 PM