How to build a protein factory? Linking structure and function of the plant endoplasmic reticulum
Lead Research Organisation:
Oxford Brookes University
Department Name: Faculty of Health and Life Sciences
Abstract
A great proportion of the planet's food supply for proteins and carbohydrates is produced, processed and transported through the plant secretory pathway. The endoplasmic reticulum (ER) forms the first compartment in the secretory pathway and is a major factory for protein and lipid synthesis, assembly, quality control, and export. The ER can also be used to produce molecules important for industry such as antibodies, therapeutics and valuable chemicals. Therefore, biotechnologically the ER has great potential for the development of strategies to manipulate or increase plant productivity. The ER forms a highly dynamic network composed of two morphologically distinct domains: sheets and tubules, which are joined at 3-way junctions to create a loose polygonal structure. The morphology of sheets and tubules has been related to different functional properties. Though both structures are present in all eukaryotic cells, the proportion of each ER structure varies between cells and species which could potentially be linked to the underlying cellular processes and the protein secretion requirements. For example, secretory cells, such as pancreatic and salivary glands, display a higher proportion of sheets. In plants two classes of proteins, reticulon and Lunapark proteins can change the ER network morphology in favour of tubules or sheets, respectively.
This project will link structure of the plant ER with ER productivity in terms of protein production and transport.
For this, we will change ER structure using ER-shaping proteins and analyse the impact of specific ER structural features such as more tubules or sheets or changes in the movement of the ER on protein production and transport.
This is an exciting project as the in-depth knowledge about ER structure and productivity will enable sustainable agricultural production of plants to cater for the planet's increasing food demands and climate change issues. The underlying mechanisms and regulations as well as the possibilities of biotechnological applications of this system will in future inform research areas such as biofuel, plant nutritional composition and pest control, biomarkers and diagnostics.
This project will link structure of the plant ER with ER productivity in terms of protein production and transport.
For this, we will change ER structure using ER-shaping proteins and analyse the impact of specific ER structural features such as more tubules or sheets or changes in the movement of the ER on protein production and transport.
This is an exciting project as the in-depth knowledge about ER structure and productivity will enable sustainable agricultural production of plants to cater for the planet's increasing food demands and climate change issues. The underlying mechanisms and regulations as well as the possibilities of biotechnological applications of this system will in future inform research areas such as biofuel, plant nutritional composition and pest control, biomarkers and diagnostics.
Technical Summary
The plant endoplasmic reticulum (ER) is the first compartment in the secretory pathway and is a major factory for protein and lipid synthesis, quality control, and export. The ER forms a highly dynamic network composed of two morphologically distinct domains: cisternae and tubules. The different morphology types have been suggested to relate to different functional properties but a convincing link has not been established yet. In plants we have two classes of proteins, reticulon and Lunapark proteins that can change the ER network morphology in favour of tubules or cisternae, respectively.
Our proposed research aims to link structure and function of the plant ER. We hypothesise that changes in ER structure and dynamics impact on ER functions and productivity focussing on protein production and transport. In particular, we will show that:
a) A more cisternal ER structure enhances protein production.
b) Changes in ER morphology affect ER to Golgi transport and secretion together with Golgi body morphology.
c) ER structural and dynamics changes affect the presence and nature of mini-tubules connecting the ER and Golgi bodies, which we suggest, are important for ER-Golgi transport.
To explore this, the project will focus on three key questions:
I) The impact of ER structure on protein production
II) The impact of ER structure on ER to Golgi protein transport
III) The impact of ER structure on secretion
This work addresses important cell biological questions but will also be of great importance to the use of plant based expression systems for therapeutics and other high-value products.
Our proposed research aims to link structure and function of the plant ER. We hypothesise that changes in ER structure and dynamics impact on ER functions and productivity focussing on protein production and transport. In particular, we will show that:
a) A more cisternal ER structure enhances protein production.
b) Changes in ER morphology affect ER to Golgi transport and secretion together with Golgi body morphology.
c) ER structural and dynamics changes affect the presence and nature of mini-tubules connecting the ER and Golgi bodies, which we suggest, are important for ER-Golgi transport.
To explore this, the project will focus on three key questions:
I) The impact of ER structure on protein production
II) The impact of ER structure on ER to Golgi protein transport
III) The impact of ER structure on secretion
This work addresses important cell biological questions but will also be of great importance to the use of plant based expression systems for therapeutics and other high-value products.
Publications
McGinness AJ
(2024)
Suborganellar resolution imaging for the localisation of human glycosylation enzymes in tobacco Golgi bodies.
in Journal of microscopy
Pain C
(2023)
intER-ACTINg: The structure and dynamics of ER and actin are interlinked.
in Journal of microscopy
Sandor A
(2024)
Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins
in Journal of Experimental Botany
Spatola Rossi T
(2023)
Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants.
in Scientific reports
Wang P
(2023)
Keep in contact: multiple roles of endoplasmic reticulum-membrane contact sites and the organelle interaction network in plants.
in The New phytologist
Description | A Community Resource for Wheat and Rice Transformation |
Amount | £1,054,979 (GBP) |
Funding ID | BB/R014876/1 |
Organisation | Biotechnology and Biological Sciences Research Council (BBSRC) |
Sector | Public |
Country | United Kingdom |
Start | 09/2018 |
End | 03/2024 |
Description | Programme Access Grant: Building blocks of a cell wall - interacting enzyme complexes in plant cell wall biosynthesis (Proposal number 2202) |
Amount | £486,000 (GBP) |
Funding ID | Building blocks of a cell wall - interacting enzyme complexes in plant cell wall biosynthesis (Proposal number 2202) |
Organisation | Research Complex at Harwell |
Sector | Public |
Country | United Kingdom |
Start | 06/2022 |
End | 07/2025 |
Description | pMMO and AMP work |
Organisation | Sheffield Hallam University |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | Ongoing work on pMMO in plants as well as antimicrobial peptides to fight plant pests. Resulted in current grant applications and PhD projects. |
Collaborator Contribution | Establishing of pMMO assays as well as AI-supported antimicrobial peptide design. Resulted in current grant applications and PhD projects. |
Impact | Resulted in current grant applications and PhD projects. |
Start Year | 2021 |
Description | Oxford Brookes Science Bazaar |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | Regional |
Primary Audience | Schools |
Results and Impact | This event is open to all. Fun for all the family and most suitable for 5-16 years. Visit us to meet our staff, students, and partner organisations, explore our interactive stands, listen to our talks, learn something new, and to get stuck into our many activities! We will be running a relaxed, autism-friendly, early-opening, 9:30am-11:30am (This session will have a limited number of visitors allowing for a quieter festival experience. When booking tickets please select the relaxed autism-friendly session.) for those who prefer a quieter festival experience. We will then be open to all from 11:30am-4pm. |
Year(s) Of Engagement Activity | 2024 |
URL | https://www.brookes.ac.uk/science-bazaar |
Description | Oxford Brookes Science Bazaar |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | Regional |
Primary Audience | Schools |
Results and Impact | This event is open to all. Fun for all the family and most suitable for 5-16 years. Visit us to meet our staff, students, and partner organisations, explore our interactive stands, listen to our talks, learn something new, and to get stuck into our many activities! We will be running a relaxed, autism-friendly, early-opening, 9:30am-11:30am (This session will have a limited number of visitors allowing for a quieter festival experience. When booking tickets please select the relaxed autism-friendly session.) for those who prefer a quieter festival experience. We will then be open to all from 11:30am-4pm. |
Year(s) Of Engagement Activity | 2024 |
URL | https://www.brookes.ac.uk/science-bazaar |