Yoshi Ichikawa
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ichikawa-lab.bsky.social
Yoshi Ichikawa
@ichikawa-lab.bsky.social
Tenure-track professor (PI) at Fudan University.
Have been working on motor protein, microtubule, and cilia.
Recently also working with membrane proteins.
Associate Editorial Board member of Cytoskeleton Journal.
Lab website: https://tinyurl.com/22c3eymy
Reposted by Yoshi Ichikawa
Our special issue on ‘Cilia and Flagella’ is now out! Huge thanks to all (authors + reviewers) who contributed, and to our wonderful Guest Editors (@cilialab.bsky.social + @lottepedersen.bsky.social) for pulling it together.
Happy reading!
#cilia #flagella

journals.biologists.com/jcs/issue/13...
Volume 138 Issue 20 | Journal of Cell Science | The Company of Biologists
Journal of Cell Science publishes cutting-edge science encompassing all aspects of cell biology. It is published by The Company of Biologists, a not-for-profit organisation.
journals.biologists.com
November 3, 2025 at 5:32 PM
Reposted by Yoshi Ichikawa
📣 Here it is — our overview on ciliary proteomics! Great discussions and writing with @mick-lab.bsky.social and Ronald Roepman 🙏🙏
Hope we didn’t miss anything important - apologies if we did!

#cilia #ciliopathies #proteomics
@theracilproject.bsky.social @for5547.bsky.social

tinyurl.com/yc8ztn5v
Advances in ciliary proteomics – towards cracking the hidden proteome code of cilia
Summary: This Review explores proteomic strategies for investigating cilia, tracing the evolution from early discoveries to recent advancements enabled by proximity labeling techniques.
journals.biologists.com
November 1, 2025 at 4:34 PM
Reposted by Yoshi Ichikawa
Miao Gui and I wrote a Review for the @jcellsci.bsky.social special issue “Cilia and Flagella: From Basic Biology to Disease”. It provides a comprehensive and up-to-date overview of MIP structure, function, and the latest tools used to study them, crafted to serve both newcomers and experts.
a man stands in front of a white board with the words keep that in mind written on it
ALT: a man stands in front of a white board with the words keep that in mind written on it
media.tenor.com
November 3, 2025 at 5:19 AM
Reposted by Yoshi Ichikawa
Ever wondered what microtubule inner proteins (MIPs) are and what they actually do? Or perhaps you already know about them, but find it hard to keep track of which ones are conserved across species and how they support ciliary structure and function?
journals.biologists.com/jcs/article/...
Microtubule inner proteins – bridging structure and function in ciliary biology
Summary: Microtubule inner proteins (MIPs) have been brought into focus by the cryo-EM revolution. This Review outlines current knowledge, emerging functions, links to ciliopathies and outstanding que...
journals.biologists.com
November 3, 2025 at 5:19 AM
A milestone reached! 1000 citations on Google Scholar!
October 30, 2025 at 4:39 PM
Reposted by Yoshi Ichikawa
Reposted by Yoshi Ichikawa
I am happy our recent study on the human sperm head-tail junction is now online. We find that SUN5 form an hexagonal lattice at the nuclear membrane, rationalising how mutations in SUN5 lead to infertility. Great work of @cryonas.bsky.social !
www.biorxiv.org/content/10.1...
SUN5 forms a regular protein lattice reinforcing the sperm head-tail junction
Linker of nucleo- and cytoskeleton (LINC) complexes reside in the nuclear envelope, the double-membrane surrounding the nucleus, where they establish a physical bridge between nucleus and cytoplasm. L...
www.biorxiv.org
July 31, 2025 at 3:07 PM
Reposted by Yoshi Ichikawa
Reposted by Yoshi Ichikawa
Excited to share our latest work with @simonbullock11.bsky.social! We looked at how diverse mRNAs get selected for subcellular localization and it turns out that a single protein can recognize different RNA elements using shared features that weren’t apparent before.
www.biorxiv.org/content/10.1...
August 5, 2025 at 10:43 AM
Reposted by Yoshi Ichikawa
Thrilled to see our study on how kinesin-2 motors are switched on and off published in @natsmb.nature.com ⚛️

➡️ www.nature.com/articles/s41...

Congrats to all authors from me and Anthony 🎉 @dunnschool.bsky.social Check out this animation made by talented PhD student @matthew-batisio.bsky.social 😆
July 29, 2025 at 9:04 AM
Reposted by Yoshi Ichikawa
Cryo-EM and biochemical reconstitution analysis reveal that Nde1 enhances Lis1 binding to autoinhibited dynein, promoting formation of a Phi-like-Lis1 intermediate during dynein activation

www.nature.com/articles/s41...
Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1 - Nature Chemical Biology
Cryo-electron microscopy and biochemical reconstitution analysis reveals that Nde1 enhances Lis1 binding to autoinhibited dynein, promoting formation of a Phi-like–Lis1 intermediate during dynein acti...
www.nature.com
August 1, 2025 at 7:52 PM
Reposted by Yoshi Ichikawa
If you’d like to join me on this journey, NBME is hiring!! This is a fantastically rewarding career that keeps you very much in science. springernature.wd3.myworkdayjobs.com/SpringerNatu...
Associate or Senior Editor, Nature Biomedical Engineering
Job Title: Associate or Senior Editor, Nature Biomedical Engineering Organization: Nature Portfolio Location: New York, Jersey City, Shanghai or Beijing – Hybrid Working Closing date: August 20, 2025 ...
springernature.wd3.myworkdayjobs.com
August 1, 2025 at 2:27 PM
Reposted by Yoshi Ichikawa
Nature Methods is also hiring to replace me (applications close August 4th!!!) and I will do everything I can to support their next bioimaging editor (ask me anything!). springernature.wd3.myworkdayjobs.com/SpringerNatu...
Associate Editor or Senior Editor, Nature Methods
Title: Associate or Senior Editor, Nature Methods Organization: Nature Portfolio Locations: New York, Jersey City, Shanghai or Beijing Closing Date: August 3, 2025    About Springer Nature Springer Na...
springernature.wd3.myworkdayjobs.com
August 1, 2025 at 2:27 PM
Reposted by Yoshi Ichikawa
🚨Last call to submit to the Forces in Cell Biology collection with @natcomms.nature.com and Scientific Reports! Deadline: 24th July

www.nature.com/collections/...
Forces in Cell Biology
Cell generate forces to maintain normal tissue morphology and function. Cells can also sense and process forces appropriate to their correct tissue context. ...
www.nature.com
July 14, 2025 at 1:17 PM
Reposted by Yoshi Ichikawa
Come work at Nature Methods! A dream job. I know from experience 😄
Nature Methods is hiring!
We are seeking a new editor with expertise in microscopy, imaging technology, and/or cell biology. The position is available in NYC/Jersey City or Shanghai/Beijing on a hybrid working model.
Apply by August 3!

springernature.wd3.myworkdayjobs.com/SpringerNatu...
a yellow sign that says we 're hiring
ALT: a yellow sign that says we 're hiring
media.tenor.com
July 10, 2025 at 12:35 PM
Reposted by Yoshi Ichikawa
New preprint from the lab - the first paper made (almost) entirely here @qmul.bsky.social

We report how human outer kinetochore complexes Ndc80 and Ska form cooperative oligomers, that together stabilise microtubule ends against shortening.
www.biorxiv.org/content/10.1...

Key results below: (1/7)
Microtubule end stabilisation by cooperative oligomers of Ska and Ndc80 complexes
During mitosis, properly aligned chromosomes stabilise microtubule ends with the help of kinetochores to ensure timely segregation of chromosomes. Microtubule-binding components of the human outer kinetochore, such as Ndc80 and Ska complexes, are present in multiple copies and together bind several microtubule ends, creating a highly multivalent binding interface. Whereas Ndc80:Ndc80 and Ndc80:microtubule binding is crucial for interface stability, Ndc80 alone in absence of Ska is unable to support stable kinetochore-attachments. Using cryoET, we demonstrate that oligomeric Ndc80:Ska assemblies stabilise microtubule ends against shortening by strengthening lateral contacts between tubulin protofilaments at microtubule plus-ends. We further identify a point mutation within the SKA1 microtubule-binding domain that does not affect microtubule-binding of individual Ska molecules, but does abolish Ska:Ska interactions. Finally, we report that oligomerisation of Ska, in a cooperative fashion together with the Ndc80, is necessary to maintain stable microtubule attachments both in vivo and in vitro. ### Competing Interest Statement The authors have declared no competing interest. BBSRC, BB/X014975/1, BB/W019698/1 Wellcome Trust, https://ror.org/029chgv08, 308895/Z/23/Z
www.biorxiv.org
July 7, 2025 at 9:39 AM
Reposted by Yoshi Ichikawa
Latest preprint from the lab, many years in the making!

By combining #cryoEM with #AlphaFold3 modelling, we propose that norovirus NS3 forms a transmembrane RNA translocase.

This could have big implications for our understanding of viral replication & assembly (🧵)

www.biorxiv.org/content/10.1...
June 18, 2025 at 6:32 AM
Reposted by Yoshi Ichikawa
Daniel's paper is now published in @jcellsci.bsky.social, great experience with @reviewcommons.org 😀

Want to know everything tubulin assembly in trypanosome flagella and other microtubules? Here is the link:

journals.biologists.com/jcs/article/...
June 12, 2025 at 8:49 AM
Reposted by Yoshi Ichikawa
SARS-CoV-2 entry captured: Cryo-ET reveals fusion intermediates of spike protein during membrane fusion, bridging stable pre- and postfusion states. PMID:40461447, Nat Commun 2025, @NatureComms https://doi.org/10.1038/s41467-025-60406-z #Medsky #Pharmsky #RNA #ASHG #ESHG 🧪
Unveiling the structural spectrum of SARS-CoV-2 fusion by in situ cryo-ET | Nature Communications
SARS-CoV-2 entry into host cells is mediated by the spike protein, which drives membrane fusion. While cryo-EM reveals stable prefusion and postfusion conformations of the spike, the transient fusion intermediate states during the fusion process remain poorly understood. Here, we design a near-native viral fusion system that recapitulates SARS-CoV-2 entry and use cryo-electron tomography (cryo-ET) to capture fusion intermediates leading to complete fusion. The spike protein undergoes extensive structural rearrangements, progressing through extended, partially folded, and fully folded intermediates prior to fusion-pore formation, a process that depends on protease cleavage and is inhibited by the WS6 S2 antibody. Upon interaction with ACE2 receptor dimer, spikes cluster at membrane interfaces and following S2’ cleavage concurrently transition to postfusion conformations encircling the hemifusion and initial fusion pores in a distinct conical arrangement. S2’ cleavage is indispensable fo
doi.org
June 4, 2025 at 10:10 AM
Reposted by Yoshi Ichikawa
🇨🇦🚨Job Alert🚨🇨🇦
Canada Excellence Research Chair (C$5 or C$10M, 8 yr budget)
U Toronto, Dept of Biochem/LabMedPath
*Was just told they're looking for a structural biologist using cryoEM* (related to infectious disease?)
Are you an established PI ready to move to 🇨🇦?
research.utoronto.ca/funding-oppo...
2026 Canada Excellence Research Chair Opportunities | Research & Innovation
research.utoronto.ca
May 31, 2025 at 12:46 PM
We were thrilled to welcome Dr. Lisa Heinke @lisaheinke.bsky.social, a Senior Editor at Nature Reviews Molecular Cell Biology, to Fudan University! She gave a fantastic talk on the editorial process and career paths as a scientific editor! Thank you, Lisa!
May 26, 2025 at 6:02 PM
Reposted by Yoshi Ichikawa
Reposted by Yoshi Ichikawa
Scientific Editor position (absence cover) - apply now and join our team!
May 17, 2025 at 6:46 AM