HaitinLab
@haitinlab.bsky.social
Located at @TelAvivUni. We study the molecular basis of information transfer within ion channels and prenyltransferases.
haitinlab.sites.tau.ac.il
haitinlab.sites.tau.ac.il
Pinned
Reposted by HaitinLab
A huge Thank You to all the collaborators who contributed to this fun project: Udi Qimron, @haitinlab.bsky.social, @bursteinlab.bsky.social, and congrats to the first author
@tridibmahata.bsky.social !
An open question remains - where will this be published? 😏
@tridibmahata.bsky.social !
An open question remains - where will this be published? 😏
two men are sitting next to each other and one of them is saying teamwork
ALT: two men are sitting next to each other and one of them is saying teamwork
media.tenor.com
September 8, 2025 at 8:13 AM
A huge Thank You to all the collaborators who contributed to this fun project: Udi Qimron, @haitinlab.bsky.social, @bursteinlab.bsky.social, and congrats to the first author
@tridibmahata.bsky.social !
An open question remains - where will this be published? 😏
@tridibmahata.bsky.social !
An open question remains - where will this be published? 😏
Reposted by HaitinLab
Great collaboration (as always)! And very funny story how HDX and native MS complement each other and reveal details about ions, substrates and mutations. We enjoyed this ride!
Excited to share our new paper in @febsj.bsky.social! 🎉
We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation
🔗 doi.org/10.1111/febs...
@peterslab1.bsky.social
We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation
🔗 doi.org/10.1111/febs...
@peterslab1.bsky.social
July 7, 2025 at 3:00 PM
Great collaboration (as always)! And very funny story how HDX and native MS complement each other and reveal details about ions, substrates and mutations. We enjoyed this ride!
Excited to share our new paper in @febsj.bsky.social! 🎉
We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation
🔗 doi.org/10.1111/febs...
@peterslab1.bsky.social
We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation
🔗 doi.org/10.1111/febs...
@peterslab1.bsky.social
July 7, 2025 at 2:36 PM
Excited to share our new paper in @febsj.bsky.social! 🎉
We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation
🔗 doi.org/10.1111/febs...
@peterslab1.bsky.social
We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation
🔗 doi.org/10.1111/febs...
@peterslab1.bsky.social
How does a cytoplasmic enzyme make a membrane product? 🤔🧬
We found that a hydrophobic residue cluster helps the human cis-prenyltransferase feed its product into the ER membrane!
MD simulations + fluorescence = mechanistic insight 👇
🔗https://doi.org/10.1002/pro.70167
We found that a hydrophobic residue cluster helps the human cis-prenyltransferase feed its product into the ER membrane!
MD simulations + fluorescence = mechanistic insight 👇
🔗https://doi.org/10.1002/pro.70167
June 2, 2025 at 7:19 PM
How does a cytoplasmic enzyme make a membrane product? 🤔🧬
We found that a hydrophobic residue cluster helps the human cis-prenyltransferase feed its product into the ER membrane!
MD simulations + fluorescence = mechanistic insight 👇
🔗https://doi.org/10.1002/pro.70167
We found that a hydrophobic residue cluster helps the human cis-prenyltransferase feed its product into the ER membrane!
MD simulations + fluorescence = mechanistic insight 👇
🔗https://doi.org/10.1002/pro.70167
But your results are 🔥 as usual!
May 11, 2025 at 5:46 PM
But your results are 🔥 as usual!
Reposted by HaitinLab
Whenever we get a bioRxiv alert, we'are always curious to see what it brings. This time, the timing couldn’t have been better - a very pleasant surprise! 😄
biorxiv.org/content/10.1...
www.biorxiv.org/content/10.1...
biorxiv.org/content/10.1...
www.biorxiv.org/content/10.1...
May 11, 2025 at 5:42 PM
Whenever we get a bioRxiv alert, we'are always curious to see what it brings. This time, the timing couldn’t have been better - a very pleasant surprise! 😄
biorxiv.org/content/10.1...
www.biorxiv.org/content/10.1...
biorxiv.org/content/10.1...
www.biorxiv.org/content/10.1...
💃🕺Happy to share a team effort to uncover the molecular "dance" behind human cis-prenyltransferase regulation!🔬🧬 @peterslab1.bsky.social @AlbGiacomello
#Biochemistry #StructuralBiology
@TAUMedFaculty @of_sagol biorxiv.org/content/10.1...
#Biochemistry #StructuralBiology
@TAUMedFaculty @of_sagol biorxiv.org/content/10.1...
Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex
Human cis-prenyltransferase (hcis-PT) synthesizes long-chain isoprenoids essential for N-linked protein glycosylation. This heteromeric complex comprises the catalytic subunit DHDDS and the regulatory...
biorxiv.org
May 11, 2025 at 1:56 PM
💃🕺Happy to share a team effort to uncover the molecular "dance" behind human cis-prenyltransferase regulation!🔬🧬 @peterslab1.bsky.social @AlbGiacomello
#Biochemistry #StructuralBiology
@TAUMedFaculty @of_sagol biorxiv.org/content/10.1...
#Biochemistry #StructuralBiology
@TAUMedFaculty @of_sagol biorxiv.org/content/10.1...
🥳
Identifying and Quantifying Membrane Interactions of the Protein Human cis-Prenyltransferase
Authors: Duncan Boren, Shiri Kredi, Ekaterina Positselskaya, Moshe Giladi, Yoni Haitin, Josh Vermaas
DOI: 10.26434/chemrxiv-2024-3gh6x
Authors: Duncan Boren, Shiri Kredi, Ekaterina Positselskaya, Moshe Giladi, Yoni Haitin, Josh Vermaas
DOI: 10.26434/chemrxiv-2024-3gh6x
January 2, 2025 at 8:34 AM
🥳
🚨New preprint alert! Wonder how a cancer-associated mutation in GGPPS impacts hexameric stoichiometry, substrate affinity, and product inhibition? Our results shed light on a novel regulatory mechanism in protein prenylation bit.ly/3ZR7w47 #MultipleMyeloma
A somatic multiple myeloma mutation unravels a mechanism of oligomerization-mediated product inhibition in GGPPS
Protein prenylation regulates the cellular localization of small GTPases and is pivotal for multiple myeloma (MM) pathology. Geranylgeranyl diphosphate synthase (GGPPS), synthesizing a prenylation moi...
bit.ly
December 26, 2024 at 9:37 AM
🚨New preprint alert! Wonder how a cancer-associated mutation in GGPPS impacts hexameric stoichiometry, substrate affinity, and product inhibition? Our results shed light on a novel regulatory mechanism in protein prenylation bit.ly/3ZR7w47 #MultipleMyeloma
Reposted by HaitinLab
1/ How do animals integrate different forms of learning? Our
@eyalrozenfeld.bsky.social new study in Science Advances
shows that active mechanisms prevent the co-formation of competing memories. Here’s what we found! 🧵👇
science.org/doi/10.1126/...
@eyalrozenfeld.bsky.social new study in Science Advances
shows that active mechanisms prevent the co-formation of competing memories. Here’s what we found! 🧵👇
science.org/doi/10.1126/...
December 8, 2024 at 6:32 AM
1/ How do animals integrate different forms of learning? Our
@eyalrozenfeld.bsky.social new study in Science Advances
shows that active mechanisms prevent the co-formation of competing memories. Here’s what we found! 🧵👇
science.org/doi/10.1126/...
@eyalrozenfeld.bsky.social new study in Science Advances
shows that active mechanisms prevent the co-formation of competing memories. Here’s what we found! 🧵👇
science.org/doi/10.1126/...
Reposted by HaitinLab
Long overlooked but significant!
This is the post-Cys specificity in post-proline cleaving enzymes like AnPEP or neprosin. Good work Zuza
and the team!🎉🔥
pubs.acs.org/doi/10.1021/...
(illustration IG:kuba_draws_science)
This is the post-Cys specificity in post-proline cleaving enzymes like AnPEP or neprosin. Good work Zuza
and the team!🎉🔥
pubs.acs.org/doi/10.1021/...
(illustration IG:kuba_draws_science)
November 21, 2024 at 9:43 AM
Long overlooked but significant!
This is the post-Cys specificity in post-proline cleaving enzymes like AnPEP or neprosin. Good work Zuza
and the team!🎉🔥
pubs.acs.org/doi/10.1021/...
(illustration IG:kuba_draws_science)
This is the post-Cys specificity in post-proline cleaving enzymes like AnPEP or neprosin. Good work Zuza
and the team!🎉🔥
pubs.acs.org/doi/10.1021/...
(illustration IG:kuba_draws_science)