HRMEM is happy to spotlight this structure of calcineurin bound to PI4KA determined by Alexandria Shaw and colleagues from the Burke Lab at the University of Victoria and the Yip Lab at UBC!
We are proud to have provided the electron microscopy for this work!
Read more:
doi.org/10.1016/j.st...
We are proud to have provided the electron microscopy for this work!
Read more:
doi.org/10.1016/j.st...
Structure of calcineurin bound to PI4KA reveals dual interface in both PI4KA and FAM126A
Phosphatidylinositol 4-kinase alpha (PI4KA) maintains the phosphatidylinositol 4-phosphate (PI4P) and phosphatidylserine pools of the plasma membrane.…
www.sciencedirect.com
May 14, 2025 at 6:30 PM
HRMEM is happy to spotlight this structure of calcineurin bound to PI4KA determined by Alexandria Shaw and colleagues from the Burke Lab at the University of Victoria and the Yip Lab at UBC!
We are proud to have provided the electron microscopy for this work!
Read more:
doi.org/10.1016/j.st...
We are proud to have provided the electron microscopy for this work!
Read more:
doi.org/10.1016/j.st...
First post up, sharing some cool work from my lab by @alexlouiseshaw.bsky.social and @sushantsuresh.bsky.social out today in Science Advances (www.science.org/doi/10.1126/...)
Molecular basis for plasma membrane recruitment of PI4KA by EFR3
The structure of the EFR3A-PI4KA complex reveals insight into PI4KA membrane localization and its role in human disease.
www.science.org
December 20, 2024 at 7:05 PM
First post up, sharing some cool work from my lab by @alexlouiseshaw.bsky.social and @sushantsuresh.bsky.social out today in Science Advances (www.science.org/doi/10.1126/...)
More structural biology! From the @jburkevic.bsky.social lab with work from @sushantsuresh.bsky.social and @alexlouiseshaw.bsky.social - featuring data collected in our facility! #cryoEM
www.jbc.org/article/S002...
www.jbc.org/article/S002...
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA
Phosphatidylinositol 4 kinase IIIα (PI4KIIIα/PI4KA) is an essential lipid kinase that
plays a critical role in regulating plasma membrane identity. PI4KA is primarily recruited
to the plasma membrane ...
www.jbc.org
November 27, 2025 at 12:55 AM
More structural biology! From the @jburkevic.bsky.social lab with work from @sushantsuresh.bsky.social and @alexlouiseshaw.bsky.social - featuring data collected in our facility! #cryoEM
www.jbc.org/article/S002...
www.jbc.org/article/S002...
Back from vacation and really glad to share some work from my PhD research. Great collaborative effort @alexlouiseshaw.bsky.social Check out this post from my PI to learn more about Lipid kinase PI4KA and its regulation!
First post up, sharing some cool work from my lab by @alexlouiseshaw.bsky.social and @sushantsuresh.bsky.social out today in Science Advances (www.science.org/doi/10.1126/...)
Molecular basis for plasma membrane recruitment of PI4KA by EFR3
The structure of the EFR3A-PI4KA complex reveals insight into PI4KA membrane localization and its role in human disease.
www.science.org
January 6, 2025 at 5:08 PM
Back from vacation and really glad to share some work from my PhD research. Great collaborative effort @alexlouiseshaw.bsky.social Check out this post from my PI to learn more about Lipid kinase PI4KA and its regulation!
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity www.biorxiv.org/content/10.64898/2026.03.06.710086v1 #cryoem
March 8, 2026 at 7:10 AM
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity www.biorxiv.org/content/10.64898/2026.03.06.710086v1 #cryoem
Final part of my PhD work is now out! We were able to develop a nanobody that inhibits EFR3 mediated PI4KA membrane recruitment. Potential therapeutic idea?
Amazing collaboration with different labs using a host of different techniques. @alexlouiseshaw.bsky.social
Amazing collaboration with different labs using a host of different techniques. @alexlouiseshaw.bsky.social
Cool new paper (www.jbc.org/article/S002... from my lab spearheaded by graduate students Sushant @sushantsuresh.bsky.social and Alex @alexlouiseshaw.bsky.social . This was a very cool collaboration with the Scott Hansen, Jennifer Cobb, Tamas Balla labs
www.jbc.org
November 6, 2025 at 12:17 AM
Final part of my PhD work is now out! We were able to develop a nanobody that inhibits EFR3 mediated PI4KA membrane recruitment. Potential therapeutic idea?
Amazing collaboration with different labs using a host of different techniques. @alexlouiseshaw.bsky.social
Amazing collaboration with different labs using a host of different techniques. @alexlouiseshaw.bsky.social
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity https://www.biorxiv.org/content/10.64898/2026.03.06.710086v1
March 8, 2026 at 3:46 AM
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity https://www.biorxiv.org/content/10.64898/2026.03.06.710086v1
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA pubmed.ncbi.nlm.nih.gov/41473329/ #cryoem
January 1, 2026 at 10:33 PM
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA pubmed.ncbi.nlm.nih.gov/41473329/ #cryoem
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA pubmed.ncbi.nlm.nih.gov/41197736/ #cryoem
November 7, 2025 at 7:10 PM
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA pubmed.ncbi.nlm.nih.gov/41197736/ #cryoem
Great collaborative work where we developed a nanobody based tool to block EFR3 mediated recruitment of PI4KA. A potential therapeutic window maybe?
Thanks @alexlouiseshaw.bsky.social for the assist!
Thanks @alexlouiseshaw.bsky.social for the assist!
New preprint from the lab headed up by
@sushantsuresh.bsky.social! Late last year, we published the molecular basis of PI4KA plasma membrane recruitment by EFR3 (PMID:39705356). This work builds on these findings and identifies a new potential therapeutic avenue! Check it out!
@sushantsuresh.bsky.social! Late last year, we published the molecular basis of PI4KA plasma membrane recruitment by EFR3 (PMID:39705356). This work builds on these findings and identifies a new potential therapeutic avenue! Check it out!
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA https://www.biorxiv.org/content/10.1101/2025.07.28.667261v1
August 7, 2025 at 5:13 AM
Great collaborative work where we developed a nanobody based tool to block EFR3 mediated recruitment of PI4KA. A potential therapeutic window maybe?
Thanks @alexlouiseshaw.bsky.social for the assist!
Thanks @alexlouiseshaw.bsky.social for the assist!
New preprint from the lab headed up by
@sushantsuresh.bsky.social! Late last year, we published the molecular basis of PI4KA plasma membrane recruitment by EFR3 (PMID:39705356). This work builds on these findings and identifies a new potential therapeutic avenue! Check it out!
@sushantsuresh.bsky.social! Late last year, we published the molecular basis of PI4KA plasma membrane recruitment by EFR3 (PMID:39705356). This work builds on these findings and identifies a new potential therapeutic avenue! Check it out!
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA https://www.biorxiv.org/content/10.1101/2025.07.28.667261v1
August 6, 2025 at 4:19 AM
New preprint from the lab headed up by
@sushantsuresh.bsky.social! Late last year, we published the molecular basis of PI4KA plasma membrane recruitment by EFR3 (PMID:39705356). This work builds on these findings and identifies a new potential therapeutic avenue! Check it out!
@sushantsuresh.bsky.social! Late last year, we published the molecular basis of PI4KA plasma membrane recruitment by EFR3 (PMID:39705356). This work builds on these findings and identifies a new potential therapeutic avenue! Check it out!
Previous work from the Reinisch and de Camilli labs had established that in mammals PI4K exists in a large trimeric complex of PI4KA-TTC7 and FAM126. However, to go to the membrane it requires interaction with another protein EFR3
December 20, 2024 at 7:08 PM
Previous work from the Reinisch and de Camilli labs had established that in mammals PI4K exists in a large trimeric complex of PI4KA-TTC7 and FAM126. However, to go to the membrane it requires interaction with another protein EFR3
A family in Spain is trying to connect people living with PI4KA-related hypomyelinating leukodystrophy in Europe. If you or your loved one is affected, and you'd like us to pass on your details, please email: info@alextlc.org
Please share 💙
#AlexTLC #HelpToCope #HelpToHope #Leukodystrophy #PI4KA
Please share 💙
#AlexTLC #HelpToCope #HelpToHope #Leukodystrophy #PI4KA
August 12, 2026 at 6:00 AM
A family in Spain is trying to connect people living with PI4KA-related hypomyelinating leukodystrophy in Europe. If you or your loved one is affected, and you'd like us to pass on your details, please email: info@alextlc.org
Please share 💙
#AlexTLC #HelpToCope #HelpToHope #Leukodystrophy #PI4KA
Please share 💙
#AlexTLC #HelpToCope #HelpToHope #Leukodystrophy #PI4KA
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity
https://www.biorxiv.org/content/10.64898/2026.03.06.710086v1
March 8, 2026 at 6:01 AM
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity
https://www.biorxiv.org/content/10.64898/2026.03.06.710086v1
Visualizing the dual interaction of calcineurin with PI4KA and FAM126A https://pubmed.ncbi.nlm.nih.gov/39515303/
November 14, 2024 at 5:39 AM
Visualizing the dual interaction of calcineurin with PI4KA and FAM126A https://pubmed.ncbi.nlm.nih.gov/39515303/
We specifically wanted this TTC7B selective nanobody to block the ability to bind EFR3, as this is the critical factor in PI4KA plasma membrane recruitment. The cryo EM structure showed a clear steric block of EFR3 binding (based on Sushant and Alex's structure from Science Advances last year)
November 5, 2025 at 10:36 PM
We specifically wanted this TTC7B selective nanobody to block the ability to bind EFR3, as this is the critical factor in PI4KA plasma membrane recruitment. The cryo EM structure showed a clear steric block of EFR3 binding (based on Sushant and Alex's structure from Science Advances last year)
Sushant and Damilola in my group were running the BLI instrument nonstop to generate all of these curves. Alex was able to solve the cryo EM structure of this nanobody bound to PI4KA-TTC7B
November 5, 2025 at 10:35 PM
Sushant and Damilola in my group were running the BLI instrument nonstop to generate all of these curves. Alex was able to solve the cryo EM structure of this nanobody bound to PI4KA-TTC7B
This is important as diseases are caused by hyperactivation of PI4KA, but complete loss is toxic. Therefore we reasoned that we might be able to selectively target unique PI4K regulatory complexes. We developed a nanobody that was highly TTC7B selective
November 5, 2025 at 10:34 PM
This is important as diseases are caused by hyperactivation of PI4KA, but complete loss is toxic. Therefore we reasoned that we might be able to selectively target unique PI4K regulatory complexes. We developed a nanobody that was highly TTC7B selective
We fully characterised all possible regulatory complexes that can form between all 6 possible combinations of PI4KA regulatory complexes containing EFR3, TTC7 and FAM126 isoforoms
November 5, 2025 at 10:32 PM
We fully characterised all possible regulatory complexes that can form between all 6 possible combinations of PI4KA regulatory complexes containing EFR3, TTC7 and FAM126 isoforoms
This focused on a long term objective in our lab, specifically understanding how the lipid kinase PI4KA is localized to the plasma membrane
PI4KA's action at the plasma membrane is critical in PM identity through the generation of the lipid PI4P
PI4KA's action at the plasma membrane is critical in PM identity through the generation of the lipid PI4P
December 20, 2024 at 7:06 PM
This focused on a long term objective in our lab, specifically understanding how the lipid kinase PI4KA is localized to the plasma membrane
PI4KA's action at the plasma membrane is critical in PM identity through the generation of the lipid PI4P
PI4KA's action at the plasma membrane is critical in PM identity through the generation of the lipid PI4P
Molecular basis for plasma membrane recruitment of PI4KA by EFR3 pubmed.ncbi.nlm.nih.gov/39705356/
December 21, 2024 at 6:24 PM
Molecular basis for plasma membrane recruitment of PI4KA by EFR3 pubmed.ncbi.nlm.nih.gov/39705356/
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA https://www.biorxiv.org/content/10.1101/2025.07.28.667261v1
August 1, 2025 at 5:45 AM
Development of an inhibitory TTC7B selective nanobody that blocks EFR3 recruitment of PI4KA https://www.biorxiv.org/content/10.1101/2025.07.28.667261v1
Molecular basis for plasma membrane recruitment of PI4KA by EFR3 https://www.biorxiv.org/content/10.1101/2024.04.30.587787v1
Molecular basis for plasma membrane recruitment of PI4KA by EFR3 https://www.biorxiv.org/content/10.1101/2024.04.30.587787v1
The lipid kinase phosphatidylinositol 4 kinase III alpha (PI4KIII/PI4KA) is a master regulator of th
www.biorxiv.org
May 1, 2024 at 5:48 AM
Molecular basis for plasma membrane recruitment of PI4KA by EFR3 https://www.biorxiv.org/content/10.1101/2024.04.30.587787v1
Structure of Calcineurin bound to PI4KA reveals dual interface in both PI4KA and FAM126A https://www.biorxiv.org/content/10.1101/2024.04.09.588654v1
Structure of Calcineurin bound to PI4KA reveals dual interface in both PI4KA and FAM126A https://www.biorxiv.org/content/10.1101/2024.04.09.588654v1
Phosphatidylinositol 4 kinase alpha (PI4KA, or PI4KIIIa), is crucial for maintaining the PI4P and ph
www.biorxiv.org
April 10, 2024 at 5:45 AM
Structure of Calcineurin bound to PI4KA reveals dual interface in both PI4KA and FAM126A https://www.biorxiv.org/content/10.1101/2024.04.09.588654v1
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity https://www.biorxiv.org/content/10.64898/2026.03.06.710086v1
March 8, 2026 at 3:46 AM
Phosphorylation of the C-terminus of PI4KA inhibits lipid kinase activity https://www.biorxiv.org/content/10.64898/2026.03.06.710086v1