Luke Neaves
-
Email
lcneav@essex.ac.uk -
Location
Colchester Campus
Profile
- Plant Biology
- Cell Biology
- Molecular Biology
- Protein-Protein interactions
- Microbiology
Biography
I am a current Specialist Technician, focusing on a project funded by a BBSRC grant to investigate novel, plant cell specific hydrogen peroxide signalling pathways between the endoplasmic reticulum and the nucleus across the perinuclear space in response to environmental stresses. To investigate this I am subjecting plant leaf material to light and heat stress conditions in order to illicit H2O2 production, which is monitored by the inoculation with the fluorescent biosensors HyPer2 and TriPer. Fluorescent microscopy images are acquired using a widefield spinning disc microscope and a light sheet microscope. I am also investigating this as a part time PhD student under the supervision of Dr Philippe Laissue and with the assistance of Prof Phil Mullineaux.
Qualifications
-
MSD (by Dissertation) in Cell and Molecular Biology University of Essex (2020)
-
BSc (Hons) in Biological Sciecnes University of Essex (2018)
Research and professional activities
Thesis
ROS signaling in plants: Are we missing a fundamental pathway?
Our concept of a convergence of H2O2 in the perinuclear space will transform our thinking and approach to linking genome-wide responses to multiple environmental challenges. Organelle-to-nucleus signaling, involving molecules such as H2O2, has been described recently as holding great potential as a target for controlling plants’ responses to fluctuating multiple stresses but only if its mechanics can be understood.
Supervisor: Dr Philippe Laissue
Research interests
Characterisation of Rhodopsin Retinitis Pigmentosa mutants located in Intradiscal Loop 1
Retinitis Pigmentosa (RP) is a genetic condition that results in blindness. There are several hundred RP mutations associated with rhodopsin, a photosensitive GPCR pigment found within rod cells of the retina. Previous studies have shown that many rhodopsin RP mutants fold incorrectly or affect protein stability. This study investigates the effect of three RP mutants located in Extracellular loop 1 of bovine rhodopsin.
