Elucidating the Cep135 - CPAP- STIL protein interaction network behind primary microcephaly and centriole formation
Lead Research Organisation:
University of Oxford
Department Name: Biochemistry
Abstract
Primary microcephaly is a hereditary disease characterised by reduced brain size from birth and mental retardation. It occurs in ~1 in 10,000 individuals in some populations, but, importantly, it is one of few diseases where we can directly trace the effects of single mutations to brain development and cognitive functions. As a result primary microcephaly cases have proved instructive in identifying crucial brain development factors for which no backup systems exist.
Centrosomes, are small organelles in human cells that organise a network of thin filaments (known as microtubules) that are essential for cells to grow, duplicate, move and sense their surroundings. Defects in centrosomes have been implicated in microcephaly. Five out of nine genes known to cause the disease correspond to centrosome components, and these include three proteins known to be essential for the formation of these organelles. In addition to microcephaly, centrosomal defects are causative agents for multiple human medical conditions, including male sterility, ciliopathies and possibly cancer. Thus, understanding how centrosomes form is an important biological question with direct medical relevance.
Over the last few years our group, and others, have shown how a single protein, SAS-6, forms the initial framework onto which centrosomes are build. Crucial to this understanding was a combination of biophysical, structural and cell biology tools that allowed us to analyse the shape of essential proteins, envision how such proteins might join to form molecular machines, and test these insights in human cells. Here, we propose to build upon our understanding of the initial centrosomal framework by studying three protein components (Cep135, CPAP and STIL) that link to it. We have selected these components because they are essential for centrosomes, they appear to be connected to one another and to SAS-6, and importantly, they are all directly implicated in primary microcephaly. We believe that understanding the role of these three proteins will also inform us on how centrosomes are formed in normal cells and how defects in them cause severe diseases. We expect that these results will underpin future efforts on how to treat such diseases.
Our group has long experience in the biophysical and structural biology methods necessary for the pursuit of this project. However, we do not rely on our core competencies alone. Our goal of understanding the centrosome structure is shared with internationally acclaimed groups in Oxford and abroad, with whom we collaborate. Our network of laboratories provides the broadest possible base of technical expertise and, thus, the best hope for determining how centrosomes form.
Centrosomes, are small organelles in human cells that organise a network of thin filaments (known as microtubules) that are essential for cells to grow, duplicate, move and sense their surroundings. Defects in centrosomes have been implicated in microcephaly. Five out of nine genes known to cause the disease correspond to centrosome components, and these include three proteins known to be essential for the formation of these organelles. In addition to microcephaly, centrosomal defects are causative agents for multiple human medical conditions, including male sterility, ciliopathies and possibly cancer. Thus, understanding how centrosomes form is an important biological question with direct medical relevance.
Over the last few years our group, and others, have shown how a single protein, SAS-6, forms the initial framework onto which centrosomes are build. Crucial to this understanding was a combination of biophysical, structural and cell biology tools that allowed us to analyse the shape of essential proteins, envision how such proteins might join to form molecular machines, and test these insights in human cells. Here, we propose to build upon our understanding of the initial centrosomal framework by studying three protein components (Cep135, CPAP and STIL) that link to it. We have selected these components because they are essential for centrosomes, they appear to be connected to one another and to SAS-6, and importantly, they are all directly implicated in primary microcephaly. We believe that understanding the role of these three proteins will also inform us on how centrosomes are formed in normal cells and how defects in them cause severe diseases. We expect that these results will underpin future efforts on how to treat such diseases.
Our group has long experience in the biophysical and structural biology methods necessary for the pursuit of this project. However, we do not rely on our core competencies alone. Our goal of understanding the centrosome structure is shared with internationally acclaimed groups in Oxford and abroad, with whom we collaborate. Our network of laboratories provides the broadest possible base of technical expertise and, thus, the best hope for determining how centrosomes form.
Technical Summary
Centrosomes are cell organelles necessary for division, motility and signalling in many species including humans. They organize the mitotic spindle, the microtubule network, cilia and flagella, and defects in their formation are linked to ciliopathies, male sterility or even cancer. Crucially, centrosomes are implicated in hereditary primary microcephaly, a bona fide genetic neurodevelopmental disorder. There, abnormalities in the timing and outcome of cell divisions by neuronal progenitor cells lead to reduced cerebral cortex size.
Centrosomes directly control crucial aspects of the cell division process, thus understanding how centrosomes, and their components, centrioles, form has attracted world-wide interest. Structural and functional studies have shown that a single protein, SAS-6, oligomerises into an initial assembly that defines the overall centriolar symmetry. However, we have relatively little mechanistic information on what follows SAS-6 oligomerisation. Here, we propose to study the essential proteins Cep135, CPAP and STIL. These proteins form an interaction network upstream of SAS-6, link to the initial SAS-6 framework and are implicated in primary microcephaly.
Our approach initially utilises protein dissection to resolve high-resolution structures (by crystallography or NMR) of individual domains and protein complexes. We then employ biophysical methods (including crosslinking assays and EM) to place the domain and complexes in the context of full-length proteins and of the whole interaction network. The structural and mechanistic insights gained in this manner will then be tested in human cells by collaborating laboratories, thereby checking the functional significance of our models.
Centrosomes directly control crucial aspects of the cell division process, thus understanding how centrosomes, and their components, centrioles, form has attracted world-wide interest. Structural and functional studies have shown that a single protein, SAS-6, oligomerises into an initial assembly that defines the overall centriolar symmetry. However, we have relatively little mechanistic information on what follows SAS-6 oligomerisation. Here, we propose to study the essential proteins Cep135, CPAP and STIL. These proteins form an interaction network upstream of SAS-6, link to the initial SAS-6 framework and are implicated in primary microcephaly.
Our approach initially utilises protein dissection to resolve high-resolution structures (by crystallography or NMR) of individual domains and protein complexes. We then employ biophysical methods (including crosslinking assays and EM) to place the domain and complexes in the context of full-length proteins and of the whole interaction network. The structural and mechanistic insights gained in this manner will then be tested in human cells by collaborating laboratories, thereby checking the functional significance of our models.
Planned Impact
We expect our activities in this project to have significant societal and economic impact in three distinct areas: (1) through direct relevance to medical conditions and improvements in human health, (2) by enhancing the education, training and career prospects of people and (3) by improving the public engagement with research.
1) Centrioles perform multiple functions in human cells including organizing the sperm flagellum, cilia in lungs, the sensory primary cilium and the mitotic spindle for all cell types. Primary microcephaly is emblematic of human diseases caused by defects in centriole formation, which also include male sterility, possibly cancer and ciliopathies. The later are an emerging class of genetic multi-symptom diseases that can affect the liver, kidneys, gut and the respiratory track. Our understanding of the molecular basis of these diseases is limited, since our knowledge of centriole formation is incomplete. Here, we aim to understand at a mechanistic level the function of centriolar proteins directly relevant to primary microcephaly, and centriole formation as a whole. We expect that the information gained could, in the future, be used by medical practitioners, for example in judging the severity of mutations identified in early embryos, and to industries aiming to provide pharmaceuticals for such diseases. Where relevant, IP protection will be sought via ISIS Innovation (a wholly owned subsidiary of the University of Oxford) to protect potentially sensitive information.
2) Basic research improves the career prospects of students and postdocs engaged in it through training and the acquisition of transferable skills. These are not limited to learning new techniques and a multi-disciplinary way of thinking; rather, they extend to mentoring people towards independence, allowing self-management and encouraging interaction and communication activities. Thus trained, researchers can engage productively in the wider knowledge economy, transfer their skills to sectors beyond academia, and assume leadership positions in their fields.
3) Increased public understanding of science is an important benefit to society as a whole. We recognize the responsibility of researchers to engage with the public and explain how expenditure in basic research underpins the economic advancement and well-being of society as a whole. In addition to creating publicly-accessible websites and authoring in blogs, our first target audience will be undergraduate students, the majority of whom radiate from academia to other sectors. By engaging undergraduates directly in our research as in point (2), and by using current research examples during teaching, we can increase their awareness, understanding and appreciation for science and its societal and economic impacts.
1) Centrioles perform multiple functions in human cells including organizing the sperm flagellum, cilia in lungs, the sensory primary cilium and the mitotic spindle for all cell types. Primary microcephaly is emblematic of human diseases caused by defects in centriole formation, which also include male sterility, possibly cancer and ciliopathies. The later are an emerging class of genetic multi-symptom diseases that can affect the liver, kidneys, gut and the respiratory track. Our understanding of the molecular basis of these diseases is limited, since our knowledge of centriole formation is incomplete. Here, we aim to understand at a mechanistic level the function of centriolar proteins directly relevant to primary microcephaly, and centriole formation as a whole. We expect that the information gained could, in the future, be used by medical practitioners, for example in judging the severity of mutations identified in early embryos, and to industries aiming to provide pharmaceuticals for such diseases. Where relevant, IP protection will be sought via ISIS Innovation (a wholly owned subsidiary of the University of Oxford) to protect potentially sensitive information.
2) Basic research improves the career prospects of students and postdocs engaged in it through training and the acquisition of transferable skills. These are not limited to learning new techniques and a multi-disciplinary way of thinking; rather, they extend to mentoring people towards independence, allowing self-management and encouraging interaction and communication activities. Thus trained, researchers can engage productively in the wider knowledge economy, transfer their skills to sectors beyond academia, and assume leadership positions in their fields.
3) Increased public understanding of science is an important benefit to society as a whole. We recognize the responsibility of researchers to engage with the public and explain how expenditure in basic research underpins the economic advancement and well-being of society as a whole. In addition to creating publicly-accessible websites and authoring in blogs, our first target audience will be undergraduate students, the majority of whom radiate from academia to other sectors. By engaging undergraduates directly in our research as in point (2), and by using current research examples during teaching, we can increase their awareness, understanding and appreciation for science and its societal and economic impacts.
Organisations
- University of Oxford (Lead Research Organisation)
- Francis Crick Institute (Collaboration)
- Swiss Federal Institute of Technology in Lausanne (EPFL) (Collaboration)
- University of Leipzig (Collaboration)
- Paul Scherrer Institute (Collaboration)
- Swiss Tropical & Public Health Institute (Collaboration)
- Birkbeck, University of London (Collaboration)
- UNIVERSITY OF CAMBRIDGE (Collaboration)
- University of Würzburg (Collaboration)
- École Polytechnique Fédérale de Lausanne (Project Partner)
People |
ORCID iD |
Ioannis Vakonakis (Principal Investigator) |
Publications
Bianchi S
(2018)
Interaction between the Caenorhabditis elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly.
in Molecular biology of the cell
Busch J
(2017)
How to Break a Ring: Exploring the Mechanisms of SAS-6 Oligomerisation
in Biophysical Journal
Busch JMC
(2020)
Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerization.
in The Journal of biological chemistry
Busch JMC
(2019)
A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6.
in Scientific reports
Day J
(2019)
The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite
in The FASEB Journal
Kantsadi AL
(2022)
Structures of SAS-6 coiled coil hold implications for the polarity of the centriolar cartwheel.
in Structure (London, England : 1993)
Machin JM
(2019)
The complex of Plasmodium falciparum falcipain-2 protease with an (E)-chalcone-based inhibitor highlights a novel, small, molecule-binding site.
in Malaria journal
Schmidt J
(2020)
Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x
in Acta Crystallographica Section F Structural Biology Communications
Warncke JD
(2016)
Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.
in Microbiology and molecular biology reviews : MMBR
Watermeyer JM
(2016)
A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum-infected erythrocytes.
in Blood
Description | Marie Sklodowska Curie Individual Fellowship |
Amount | £183,454 (GBP) |
Funding ID | 752069 |
Organisation | European Commission |
Sector | Public |
Country | European Union (EU) |
Start | 07/2017 |
End | 06/2019 |
Title | Chemical shift assignments of PfEMP1 ATSCore - variant PFF0845c |
Description | Chemical shift assignments of PfEMP1 ATSCore - variant PFF0845c |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight into malaria virulence complex formation |
URL | http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26772 |
Title | Chemical shift assignments of Spectrin repeat a17 |
Description | Chemical shift assignments of Spectrin repeat a17 |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight in formation of malaria virulence complex |
URL | http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=26773 |
Title | Crystal structure of the Danio rerio centrosomal protein Cep135 coiled-coil fragment 64-190 |
Description | Crystallographic structure of the D. rerio Cep135 coiled-coil fragment |
Type Of Material | Database/Collection of data |
Year Produced | 2021 |
Provided To Others? | Yes |
Impact | No impacts thus far |
URL | https://www.rcsb.org/structure/7BJI |
Title | Crystallographic structure of PFA0660w J-domain |
Description | Crystallographic structure of PFA0660w J-domain |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight on co-chaperone function in PfHsp70-x activation |
URL | http://www.rcsb.org/structure/6RZY |
Title | Crystallographic structure of PfHsp70-x - ADP form |
Description | Crystallographic structure of PfHsp70-x - ADP form |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight in PfHsp70-x function |
URL | http://www.rcsb.org/structure/6S02 |
Title | Crystallographic structure of PfHsp70-x - ANPPnP form |
Description | Crystallographic structure of PfHsp70-x - ANPPnP form |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight on function of PfHsp70-x |
URL | http://www.rcsb.org/structure/6RZQ |
Title | Crystallographic structure of human alpha spectrin domains 16-17 |
Description | Crystallographic structure of human spectrin alpha16-17 |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight on malaria virulence complex formation process |
URL | http://www.rcsb.org/structure/5J4O |
Title | Electron tomography - Detergent-insoluble skeleton of Plasmodium falciparum schizont |
Description | Electron tomography - Detergent-insoluble skeleton of Plasmodium falciparum schizont |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight in formation of malaria virulence complex |
URL | https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-3123 |
Title | Electron tomography - Detergent-insoluble skeleton of Plasmodium falciparum schizont, labelled with anti-KAHRP antibody |
Description | Electron tomography - Detergent-insoluble skeleton of Plasmodium falciparum schizont, labelled with anti-KAHRP antibody |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight into formation of malaria virulence complex |
URL | https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-3122 |
Title | Electron tomography - Detergent-insoluble skeleton of human erythrocyte |
Description | Electron tomography - Detergent-insoluble skeleton of human erythrocyte |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight into formation of malaria virulence complex |
URL | https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-3117 |
Title | Electron tomography - Detergent-resistant skeleton of P. falciparum schizont |
Description | Electron tomography - Detergent-resistant skeleton of P. falciparum schizont |
Type Of Material | Database/Collection of data |
Year Produced | 2017 |
Provided To Others? | Yes |
Impact | Insight into formation of malaria virulence complex |
URL | https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-3116 |
Title | NMR chemical shifts of C. elegans SAS-5 N-terminus |
Description | Sequence-specific NMR chemical shift assignments of the C. elegans SAS-5 N-terminal, microtubule-interacting domain |
Type Of Material | Database/Collection of data |
Year Produced | 2018 |
Provided To Others? | Yes |
Impact | Facilitated the characterisation of the SAS-5 / microtubule interaction |
URL | http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=27056 |
Title | Sequence specific chemical shift assignments of the Caenorhabditis elegans SAS-6 N-terminal domain |
Description | Sequence specific chemical shift assignments of the Caenorhabditis elegans SAS-6 N-terminal domain |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight in centriole formation process |
URL | http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=27607 |
Title | Sequence-specific assignments of Plasmodium falciparum PFE0055c J-domain |
Description | Sequence-specific assignments of Plasmodium falciparum PFE0055c J-domain |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight into PfHsp70-x function |
URL | http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=27953 |
Title | Sequence-specific assignments of the P. falciparum PFE0660w J-domain |
Description | Sequence-specific assignments of the P. falciparum PFE0660w J-domain |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight into malaria PfHsp70-x function |
URL | http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=27952 |
Title | Sequence-specific resonance assignments of the Chlamydomonas reinhardtii SAS-6 N-terminal domain, F145E variant |
Description | NMR chemical shift assignment of the C. reinhardtii SAS-6 N-terminal domain |
Type Of Material | Database/Collection of data |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | Datasets used for publication |
URL | https://bmrb.io/data_library/summary/index.php?bmrbId=50300 |
Title | Sequence-specific resonance assignments of the human SAS-6 F131D head domain |
Description | NMR chemical shift assignments of the human SAS-6 N-terminal domain |
Type Of Material | Database/Collection of data |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | Dataset used in publication |
URL | https://bmrb.io/data_library/summary/index.php?bmrbId=50308 |
Title | Structure of FCP in complex with novel inhibitor |
Description | Structure of FCP protein in complex with novel inhibitor, resolved by X-ray crystallography |
Type Of Material | Database/Collection of data |
Year Produced | 2019 |
Provided To Others? | Yes |
Impact | Insight on FCP mode of inhibition |
URL | http://www.rcsb.org/structure/6SSZ |
Title | Structure of the Plasmodium falciparum Hsp70-x substrate binding domain in complex with hydrophobic peptide |
Description | Crystal structure of the P. falciparum Hsp70x chaperone SBD in complex with peptide |
Type Of Material | Database/Collection of data |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | Dataset used in publication |
URL | https://www.rcsb.org/structure/6ZHI |
Title | Structure of the human SAS-6 N-terminal domain, F131E mutant |
Description | Crystal structure of the human SAS-6 head domain |
Type Of Material | Database/Collection of data |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | Dataset used in publication |
URL | https://www.rcsb.org/structure/6Z4A |
Description | Oxford - Birkbeck - Crick collaboration |
Organisation | Birkbeck, University of London |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | Biophysical insight on interactions of malaria parasite proteins. |
Collaborator Contribution | Electron microscopy (Birkbeck - Prof. Saibil) and in cellulo (Crick - Dr. Blackman) assays in support of our biophysical insights. |
Impact | Joint research publication with Saibil and Blackman groups. |
Start Year | 2013 |
Description | Oxford - Birkbeck - Crick collaboration |
Organisation | Francis Crick Institute |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | Biophysical insight on interactions of malaria parasite proteins. |
Collaborator Contribution | Electron microscopy (Birkbeck - Prof. Saibil) and in cellulo (Crick - Dr. Blackman) assays in support of our biophysical insights. |
Impact | Joint research publication with Saibil and Blackman groups. |
Start Year | 2013 |
Description | Oxford - EPFL collaboration |
Organisation | Swiss Federal Institute of Technology in Lausanne (EPFL) |
Country | Switzerland |
Sector | Public |
PI Contribution | We have developed a collaboration with a group at the EPFL, Switzerland, to evaluate structural insights in cellular systems. |
Collaborator Contribution | In vivo and in cellulo assays in support of structural insights gained for centriolar proteins. |
Impact | Joint research publications with Prof. Gonczy |
Start Year | 2010 |
Description | Oxford - LMB collaboration |
Organisation | University of Cambridge |
Department | Department of Genetics |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | Provision of recombinant protein samples from our laboratory to that of Prof. David Glover. Sharing of unpublished information on centriolar protein structure. |
Collaborator Contribution | Sharing of unpublished information on centriolar protein interactions. Provision of genetic constructs for our laboratory. |
Impact | No outputs to date. Multidisciplinary collaboration between structural biology and biophysics (our group) and cell biologists (Prof. Glover). |
Start Year | 2017 |
Description | Oxford - Leipzig collaboration |
Organisation | University of Leipzig |
Country | Germany |
Sector | Academic/University |
PI Contribution | Structural insights on role of neuronal synapse proteins. |
Collaborator Contribution | In vivo assays testing our structural insights. Work with Prof. Langenhan (previously at University of Wurzburg, Germany). |
Impact | No published outcomes yet. |
Start Year | 2015 |
Description | Oxford - SwissTPH collaboration |
Organisation | Swiss Tropical & Public Health Institute |
Country | Switzerland |
Sector | Academic/University |
PI Contribution | Provide structural insights in the role of malaria parasite proteins. |
Collaborator Contribution | In cellulo assays to test our structural insights. Work performed with Profs. Beck and Voss. |
Impact | Joint research publications with Prof. Beck. |
Start Year | 2011 |
Description | Oxford - Wurzburg collaboration |
Organisation | University of Wurzburg |
Country | Germany |
Sector | Academic/University |
PI Contribution | Structural insights on role of neuronal synapse proteins. |
Collaborator Contribution | Electrophysiology and in vivo assays testing our structural insights. Work with (formerly) Prof. Langenhan and (currently) Prof. Heckmann. |
Impact | No published outputs yet. |
Start Year | 2012 |
Description | Oxford-PSI collaboration |
Organisation | Paul Scherrer Institute |
Country | Switzerland |
Sector | Academic/University |
PI Contribution | Collaboration with a group at the Paul Scherrer Institut, Switzerland, for electron microscopy |
Collaborator Contribution | EM and in cellulo studies of microtubule binding in support of structural insights from centriolar proteins. |
Impact | Joint research publications with group of Prof. Steinmetz |
Start Year | 2010 |
Description | Invited presentation at the University of Zurich - Switzerland |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Postgraduate students |
Results and Impact | Invited presentation on group research on centriolar proteins at the University of Zurich - Department of Chemistry |
Year(s) Of Engagement Activity | 2019 |
Description | Oxford Open Days |
Form Of Engagement Activity | Participation in an open day or visit at my research institution |
Part Of Official Scheme? | No |
Geographic Reach | National |
Primary Audience | Public/other audiences |
Results and Impact | Open Days in Oxford Biochemistry, targeting prospective undergraduate students as well as their parents. The Open Days feature a mixture of face-to-face meetings, research demos, and organised talks. |
Year(s) Of Engagement Activity | 2013,2014,2015,2016,2017,2018,2019 |
Description | Research talk to prospective DPhil students |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | Local |
Primary Audience | Postgraduate students |
Results and Impact | Research talks to prospective structural biology DPhil students to inform their decisions on which research topic(s) to devote their studies on. Two students decided to do their PhDs on centriole biology. |
Year(s) Of Engagement Activity | 2012,2013,2014,2015 |
Description | School outreach |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | Local |
Primary Audience | Schools |
Results and Impact | Presentation of research demos to 30-60 primary school children. The children were engaged directly by asking them to participate (i.e. perform) some simple chemistry experiments. |
Year(s) Of Engagement Activity | 2017,2018 |
Description | Talk at UCL - Birbeck |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | National |
Primary Audience | Postgraduate students |
Results and Impact | Talk on centriolar research at UCL / Birbeck, London |
Year(s) Of Engagement Activity | 2016 |
Description | Talk at the Structural Biology 2017 conference |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Other audiences |
Results and Impact | Invited presentation at the Structural Biology 2017 conference in Zurich, Switzerland, Sept. 18-20 2017 |
Year(s) Of Engagement Activity | 2017 |
URL | https://structuralbiology.conferenceseries.com/2017/ |
Description | Undergraduate research presentations |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | Local |
Primary Audience | Undergraduate students |
Results and Impact | Recruited two undergraduate students to work on this project Helped undergraduate students decide what research to pursue as part of their Biochemistry degree. |
Year(s) Of Engagement Activity | 2012,2013,2014,2015,2016,2017,2018,2019 |