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Kota Saito

@saitolab.bsky.social
37 followers 43 following 5 posts

Akita University, Graduate School of Medicine Cell Biology, ER exit site, Secretion, Collagen

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Kota Saito @saitolab.bsky.social · 17/09/2026
Our collaborative paper is now out in Matrix Biology! We made TANGO1L KO cells and analyzed them extensively. TANGO1L Is Required for Collagen Secretion in a Type-Dependent Manner and Shapes Collagen Proteostasis in the Endoplasmic Reticulum. doi.org/10.1016/j.ma...
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Reposted by Kota Saito
Bio-protocol @bio-protocol.bsky.social · 07/01/2026
Detecting the Activation of Endogenous Small GTPases via Fluorescent Signals Utilizing a Split mNeonGreen Work by Miharu Maeda and Kota Saito at Akita University. #LifeSciences #Reproducibility #CellBiology
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Kota Saito @saitolab.bsky.social · 13/12/2025
Detecting the Activation of Endogenous Small GTPases via Fluorescent Signals Utilizing a Split mNeonGreen: Small GTPase ActIvitY ANalyzing (SAIYAN) System bio-protocol.org/en/bpdetail?...
bio-protocol.org
Detecting the Activation of Endogenous Small GTPases via Fluorescent Signals Utilizing a Split mNeonGreen: Small GTPase ActIvitY ANalyzing (SAIYAN) System
Small GTPases function as molecular switches in cells, and their activation triggers diverse cellular responses depending on the GTPase type. Therefore, visualizing small GTPase activation in living c...
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Reposted by Kota Saito
Cell Biology J-Club @cellclub.bsky.social · 25/11/2025
Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites www.nature.com/articles/s41...
nature.com
Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites - Nature Communications
The ER exit site is a portal on the endoplasmic reticulum where secretory proteins depart. Here, the authors revealed that a balanced phosphorylation state of the ER exit site proteins TANGO1 and Sec1...
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Reposted by Kota Saito
Ishier Raote @ishier.bsky.social · 25/11/2025
Nice paper from Kota @saitolab.bsky.social! Balanced phosphorylation of TANGO1 and Sec16A keep ER exit sites stable and functional. Do cells maintain this dynamically to keep secretory machinery primed and responsive to changing cargo loads or environmental signals? www.nature.com/articles/s41...
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Kota Saito @saitolab.bsky.social · 26/11/2025
Our paper is now out in Nature Communications! Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites. rdcu.be/eRNLt TANGO1 and Sec16 need a Goldilocks level of phosphorylation — not too high, not too low.
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Reposted by Kota Saito
Lisa Heinke @lisaheinke.bsky.social · 30/09/2025
Check out this new Roadmap, a fantastic team effort by a consortium of ER researchers. Glad we could provide the space for this synthesis, which came out of discussions at a fruitful meeting, see below:
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Reposted by Kota Saito
Nature Reviews Molecular Cell Biology @natrevmcb.nature.com · 29/09/2025
New Online! Towards a unified framework for the function of endoplasmic reticulum exit sites
bit.ly
Towards a unified framework for the function of endoplasmic reticulum exit sites
Nature Reviews Molecular Cell Biology, Published online: 29 September 2025; doi:10.1038/s41580-025-00899-0Endoplasmic reticulum exit sites (ERES) are specialized ER subdomains that regulate the export of secreted cargo. This Roadmap explores how ERES integrate biochemical and mechanical signals to coordinate trafficking and proposes a multidisciplinary strategy to investigate their function, including in disease.
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Kota Saito @saitolab.bsky.social · 31/07/2025
Our lab website has been updated!  ksaitolab.com
ksaitolab.com
Saito Lab|Akita University
Department of Biological Informatics and Experimental Therapeutics Graduate School of Medicine, Akita University 秋田大学 大学院医学系研究科 情報制御学・実験治療学講座(旧薬理学講座)
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Reposted by Kota Saito
bioRxiv Cell Biology @biorxiv-cellbio.bsky.social · 20/06/2025
Phosphorylation-Coupled Autoregulation Maintains Functional ER Exit Sites www.biorxiv.org/content/10.1101/202…
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Kota Saito @saitolab.bsky.social · 20/06/2025
This is my first post. We are very happy to share the following preprint! Our work introduces a novel concept that the functional state of the ERES is maintained through the autoregulated phosphorylation–dephosphorylation cycle of key scaffold proteins. www.biorxiv.org/content/10.1...
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