Kota Saito
@saitolab.bsky.social
Akita University, Graduate School of Medicine Cell Biology, ER exit site, Secretion, Collagen
【注目プレスリリース】コラーゲン分泌の鍵を握る受容体タンパク質TANGO1Lの解析 ～コラーゲンの種類に応じた適応的応答を明らかに～ / 秋田大学 https://research-er.jp/articles/view/160592
コラーゲン分泌の鍵を握る受容体タンパク質TANGO1Lの解析 ～コラーゲンの種類に応じた適応的応答を明らかに～
2026.10.05 秋田大学 プレスリリース 秋田大学(学長:南谷佳弘)大学院医学系研究科薬理学講座の齋藤康太教授、前田深春講師らの研究グループは、カリフォルニ...
research-er.jp
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...
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
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?...
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...
bio-protocol.org
Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites www.nature.com/articles/s41...
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...
nature.com
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...
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.
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:
Ishier Raote@ishier.bsky.social · last yr.ER exit sites are dynamic ER subdomains that integrate signals, reshape membranes and steer secretion. Twelve groups in the field came together to map their diversity, regulation, unanswered questions and future directions. www.nature.com/articles/s41...
New Online! Towards a unified framework for the function of endoplasmic reticulum exit sites
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.
bit.ly
Phosphorylation-Coupled Autoregulation Maintains Functional ER Exit Sites https://www.biorxiv.org/content/10.1101/2025.06.18.660491v1
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...
