Dr Clinton Lau

MBiochem, DPhil Oxf

Stipendiary Lecturer

I moved from Leeds to read Biochemistry at the University of Oxford for my undergraduate degree, studying at New College. During this time I became fascinated at the diversity of structure and function of the molecular machines that underpin life. For my DPhil in the Higgins Lab, I studied how diverse proteins from the malaria parasite, Plasmodium falciparum, interact with a particular human receptor. I then moved to Cambridge to work with Andrew Carter at the MRC LMB. Here I sought to understand how the molecular motor dynein can bind its diverse cargos, which get transported vast distances within cells. Through these previous positions I gained structural biology tools such as cryo-EM, as well as techniques to study protein function in vitro such as single-molecule TIRF assays. I now run a lab in the Department of Biochemistry to research how the malaria-causing parasite, Plasmodium falciparum, uses cytoskeletal filaments to organise its cellular components, in addition to teaching roles in the College and Department.

I give lectures on protein purification and parasitology, and give tutorials relating to aspects of protein structure and function.

 

I run a lab in the Department of Biochemistry to research how the malaria-causing parasite, Plasmodium falciparum, uses cytoskeletal filaments to organise its cellular components. We seek to understand the structure and function of these components using techniques such as single particle cryo-electron microscopy and single-molecule TIRF microscopy.

https://laulab.web.ox.ac.uk/

AI told you so: navigating protein structure prediction in the era of machine learning. Sami Chaaban, Giedrė Ratkevičiūtė, Clinton Lau; Biochem (Lond) 2024; doi: https://doi.org/10.1042/bio_2024_118

Molecular mechanism of dynein-dynactin complex assembly by LIS1. Singh K*, Lau CK*, Manigrasso G, Gama JB, Gassmann R, Carter AP. Science. 2024 Mar 29; https://doi.org/10.1126/science.adk8544.

Cryo-EM reveals the complex architecture of dynactin’s shoulder and pointed end. Lau CK, O’Reilly FJ, Santhanam B, Lacey SE, Rappsilber J, Carter AP. EMBO J. 2021 Mar 18;e106164.

Shulin packages axonemal outer dynein arms for ciliary targeting. Mali GR*, Abid Ali F*, Lau CK*, Begum F, Boulanger J, Howe JD, Chen ZA, Rappsilber J, Skehel M, Carter AP. Science. 2021 Feb 26;371(6532):910-916.

Cryo-EM shows how dynactin recruits two dyneins for faster movement. Urnavicius L*, Lau CK*, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP. Nature. 2018 Feb 7;554(7691):202-206.

Structural conservation despite huge sequence diversity allows EPCR binding by the PfEMP1 family implicated in severe childhood malaria. Lau CK*, Turner L*, Jespersen JS, Lowe ED, Petersen B, Wang CW, Petersen JE, Lusingu J, Theander TG, Lavstsen T, Higgins MK. Cell Host Microbe. 2015 Jan 14;17(1):118-29.

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