Pedro Latorre-Muro
platorremuro.bsky.social
Pedro Latorre-Muro
@platorremuro.bsky.social
Scientist. Veterinarian. Spaniard. Curiosity drives change. Instructor DFCI_CancerBio & HarvardCellBio. K99 Awardee NIDDK. Previous HFSP fellow.
Reposted by Pedro Latorre-Muro
Now out in Science! Cyclin-dependent kinases (CDKs) are key regulators of the cell cycle. In @vcushing.bsky.social's magnum opus, we use #cryoEM to figure out how the CDK-activating kinase recognises CDKs to fully activate them - a key step in cell cycle control.
www.science.org/doi/10.1126/...
Structural basis of T-loop–independent recognition and activation of CDKs by the CDK-activating kinase
Cyclin-dependent kinases (CDKs) are prototypical regulators of the cell cycle. The CDK-activating kinase (CAK) acts as a master regulator of CDK activity by catalyzing the activating phosphorylation o...
www.science.org
October 16, 2025 at 7:17 PM
Reposted by Pedro Latorre-Muro
Our paper showing that ergothioneine controls mitochondrial function and exercise performance via direct activation of MPST is now published @cp-cellmetabolism.bsky.social

Thanks to everyone involved!

www.cell.com/cell-metabol...
February 17, 2025 at 5:33 PM
Reposted by Pedro Latorre-Muro
💫NEW by @ppuigserverb.bsky.social & co: the chaperone PPID drives insertion of the #mitochondria import receptor TOM70 into the mitochondrial outer membrane, regulating body temperature, glucose homeostasis and body weight in #obese mice.
👉https://rdcu.be/d8atv
www.nature.com/articles/s41...
Chaperone-mediated insertion of mitochondrial import receptor TOM70 protects against diet-induced obesity - Nature Cell Biology
Latorre-Muro et al. show that the cytosolic chaperone PPID drives insertion of the mitochondrial import receptor TOM70 into the mitochondrial outer membrane, thereby regulating body temperature, gluco...
www.nature.com
January 31, 2025 at 1:39 PM
Very exciting findings @ppuigserverb.bsky.social connect mitochondrial ETC deficiencies with cancer cell immunogenicity expanding the repertoire of strategies to target tumor vulnerabilities
January 24, 2025 at 6:09 PM
Reposted by Pedro Latorre-Muro
New studies from our lab by Tevis Vitale and Jason Liang in @naturecancer.bsky.social Selective deficiency of complex I subunits causes tumor immunogenicity via T cell surveillance and Immune Checkpoint Blockade responsiveness Collaboration with Widlund, Gygi and Wucherpfennig labs rdcu.be/d6BgJ
January 17, 2025 at 11:16 AM
Very excited to start 2025 sharing our latest work @ppuigserverb.bsky.social published in @naturecellbiology.bsky.social! We have shown that the cytosolic chaperone PPID/CYP40 inserts TOM70, connecting chaperones and mitochondrial protein biogenesis to the development of chronic metabolic disorders
New article by @platorremuro.bsky.social published in @naturecellbiology.bsky.social Chaperone-mediated insertion of mitochondrial import receptor TOM70 protects against diet-induced obesity- With Kajimura, Gygi and Eck labs @danafarber.bsky.social @harvardcellbio.bsky.social
rdcu.be/d5ptF
January 3, 2025 at 3:29 PM
Reposted by Pedro Latorre-Muro
Thrilled to share our new paper @Chouchani Lab in Cell; what a great way to end this year! We establish a deep mapping of the zinc-binding human cysteine proteome (ZnCPT) and discover glutathione reductase as zinc-targetable cancer vulnerability. www.cell.com/cell/fulltex...
The human zinc-binding cysteine proteome
A deep mapping of the human zinc-binding cysteine proteome (ZnCPT) defines thousands of zinc-binding protein cysteines across major domains of biology and discovers glutathione reductase as zinc-targetable cancer vulnerability.
www.cell.com
December 31, 2024 at 4:21 PM
Reposted by Pedro Latorre-Muro
Our recent work on mitochondrial respiratory complexes @platorremuro.bsky.social highlighted in the DFCI Inside blog- Thanks to the Dana-Farber Editorial team for written this blog @danafarber.bsky.social
blog.dana-farber.org/insight/2024...
December 19, 2024 at 5:33 PM
Reposted by Pedro Latorre-Muro
In the latest issue of Cell- Structural basis of respiratory complex adaptation to cold temperatures
Structural basis of respiratory complex adaptation to cold temperatures
High-resolution structures of respiratory I:III2 complexes from brown fat adapted to cold temperatures reveal a distinct supercomplex assembly with rotated CIII2 that displays higher electron transfer...
www.cell.com
November 18, 2024 at 1:49 PM