Proteomics Approaches to Map the Three-Dimensional Cell
1:00pm - 2:00pm /
Monday 22nd October 2018
/ Venue: Lecture Theatre 2 Life Sciences Building
- Rob Beynon
- Suitable for: Staff and students with an interest in biochemistry
- Admission: Free
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Speaker: Kathryn Lilley (Cambridge Centre for Proteomics)
Proteins can adopt multiple functions controlled by their sub-cellular location, binding partners and post transcriptional and post translational modification status, and structure. Such differential control significantly increases the functionality of the proteome over what is encoded by the genome. The processes governing these features are highly dynamic and their aberrant control is implicated in many diseases.
We have developed methods to determine the three dimensional organisation of the proteome in eukaryote cells in a single experiment with very good resolution (Mulvey et al, Nature Protocols (2017)). We have applied this method to many different biological systems, including mapping protein relocalization upon perturbation. In all cases, an intriguing observation is that up to half the proteome resides in more than one place. This observation has been recently supported by comparing two very different approaches to map proteins to different subcellular niches (Thul et al, Science (2017)).
In this lecture I will review methodologies that can be used to capture spatial information about the proteome. I will also introduce quantitative mass spectrometry methods that support some of these approaches. Finally I will introduce a new method that also allows us add another layer of complexity upon spatial maps; the location of interaction of the transcriptome and proteome.
Proteins can adopt multiple functions controlled by their sub-cellular location, binding partners and post transcriptional and post translational modification status, and structure. Such differential control significantly increases the functionality of the proteome over what is encoded by the genome. The processes governing these features are highly dynamic and their aberrant control is implicated in many diseases.
We have developed methods to determine the three dimensional organisation of the proteome in eukaryote cells in a single experiment with very good resolution (Mulvey et al, Nature Protocols (2017)). We have applied this method to many different biological systems, including mapping protein relocalization upon perturbation. In all cases, an intriguing observation is that up to half the proteome resides in more than one place. This observation has been recently supported by comparing two very different approaches to map proteins to different subcellular niches (Thul et al, Science (2017)).
In this lecture I will review methodologies that can be used to capture spatial information about the proteome. I will also introduce quantitative mass spectrometry methods that support some of these approaches. Finally I will introduce a new method that also allows us add another layer of complexity upon spatial maps; the location of interaction of the transcriptome and proteome.