Kota Saito
@saitolab.bsky.social
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Akita University, Graduate School of Medicine Cell Biology, ER exit site, Secretion, Collagen
pinned post!
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.
about 1 month ago
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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?...
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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...
https://bio-protocol.org/en/bpdetail?id=5557&type=0
17 days ago
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reposted by
Kota Saito
Cell Biology J-Club
about 1 month ago
Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites
www.nature.com/articles/s41...
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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...
https://www.nature.com/articles/s41467-025-65409-4
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reposted by
Kota Saito
Ishier Raote
about 1 month ago
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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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.
about 1 month ago
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4
3
reposted by
Kota Saito
Lisa Heinke
3 months ago
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:
add a skeleton here at some point
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reposted by
Kota Saito
Nature Reviews Molecular Cell Biology
3 months ago
New Online! Towards a unified framework for the function of endoplasmic reticulum exit sites
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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.
https://bit.ly/4nRmf9B
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Our lab website has been updated!
ksaitolab.com
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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)
https://ksaitolab.com/
5 months ago
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reposted by
Kota Saito
bioRxiv Cell Biology
6 months ago
Phosphorylation-Coupled Autoregulation Maintains Functional ER Exit Sites
https://www.biorxiv.org/content/10.1101/2025.06.18.660491v1
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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...
6 months ago
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