Author

Lucas Albacete-Albacete

MRC Laboratory of Molecular BiologyORCID 0000-0001-7464-1845Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Cell Biology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

Simon L. BullockiD· 2 shared Christopher S. FraseriD· 1 shared Eve MehtabiD· 1 shared Irene Díaz‐LópeziD· 1 shared Jailson Brito QueridoiD· 1 shared Jérôme Boulanger AiD· 1 shared Li Jin· 1 shared Mark A McClintockiD· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersCell Biology

Simon L. BullockORCID

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3 papers

Recent·Most cited

FXR proteins and BICD2 cooperate to promote dynein-mediated RNP transport and stress granule assembly

Yaiza Andrés Jeske, Eve Mehtab, Lucas Albacete-Albacete, Mark A McClintock, Jérôme Boulanger A, Simon L. Bullock

This study shows that FXR proteins and BICD2 work together to activate dynein for RNP transport and stress granule formation, revealing separable steps in dynein-mediated transport.

bioRxiv · Sep 28, 2026 · PreprintCell Biology

Dynein-dependent positioning of multiple organelles regulates adaptive gene expression during oxidative stress

Lucas Albacete-Albacete, Li Jin, Nanami Sato, Marta N. Shahbazi, Simon L. Bullock

The paper shows that dynein-dependent organelle clustering during oxidative stress enhances gene expression by coordinating organelle positioning.

bioRxiv · Mar 17, 2026 · PreprintCell Biology

Human tumor suppressor protein Pdcd4 binds at the mRNA entry channel in 40S small ribosomal subunit

Jailson Brito Querido, Masaaki Sokabe, Irene Díaz‐López, Yuliya Gordiyenko, Philipp Konrad Zuber, Yifei Du, Lucas Albacete-Albacete, Venki Ramakrishnan, Christopher S. Fraser

This study determines the structure of Pdcd4 bound to the 40S ribosomal subunit, revealing its binding site and mechanism in translational control.

Nature Communications · Aug 8, 2024Peer-reviewedBiochemistry