Kota Saito
@saitolab.bsky.social
Akita University, Graduate School of Medicine
Cell Biology, ER exit site, Secretion, Collagen
Cell Biology, ER exit site, Secretion, Collagen
Pinned
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.
TANGO1 and Sec16 need a Goldilocks level of phosphorylation — not too high, not too low.
Reposted by Kota Saito
Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites
www.nature.com/articles/s41...
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...
www.nature.com
November 25, 2025 at 2:54 PM
Phosphorylation-coupled autoregulation of TANGO1 and Sec16A maintains functional ER exit sites
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Reposted by Kota Saito
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...
Do cells maintain this dynamically to keep secretory machinery primed and responsive to changing cargo loads or environmental signals?
www.nature.com/articles/s41...
November 25, 2025 at 4:22 PM
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...
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.
TANGO1 and Sec16 need a Goldilocks level of phosphorylation — not too high, not too low.
November 26, 2025 at 4:53 AM
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.
TANGO1 and Sec16 need a Goldilocks level of phosphorylation — not too high, not too low.
Reposted by Kota Saito
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:
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...
www.nature.com/articles/s41...
Towards a unified framework for the function of endoplasmic reticulum exit sites - Nature Reviews Molecular Cell Biology
Endoplasmic 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.
www.nature.com
September 30, 2025 at 7:35 AM
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:
Reposted by Kota Saito
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
September 29, 2025 at 6:31 PM
New Online! Towards a unified framework for the function of endoplasmic reticulum exit sites
Our lab website has been updated! 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）
ksaitolab.com
July 31, 2025 at 1:44 AM
Our lab website has been updated! ksaitolab.com
Reposted by Kota Saito
Phosphorylation-Coupled Autoregulation Maintains Functional ER Exit Sites https://www.biorxiv.org/content/10.1101/2025.06.18.660491v1
June 20, 2025 at 10:30 AM
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...
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...
June 20, 2025 at 9:22 PM
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...
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...