Dr Benjamin Lane

Supervisor Details

Contact Details

Scientific Background

Research Interests

My research uses structural biology approaches to understand the structure and mechanisms of membrane proteins, utilising cryo-electron microscopy alongside complementary techniques. A central theme is understanding the involvement of protein-lipid interactions in membrane protein mechanisms, and how these interactions might be exploited as antimicrobial strategies in the future.

Research Groups

Aston Institute for Membrane Excellence

Supervision Style

In three words or phrases: Supportive, student-centred, collaborative.

Provision of Training

I prefer to take responsibility for your technical training at first, leading to more independence later.

Progression Monitoring and Management

I will expect you to take full ownership of your project, but I like to be kept up to date through weekly meetings. I am here for advice and guidance to help you reach the goals we set together.

Communication

I like to meet in person when at all possible. I am often available in person or via email for a response within a short period of time. I sometimes email out of hours, however I will not expect you to do the same.

PhD Students can expect scheduled meetings with me:

In a group meeting

At least once a week

In year 1 of PhD study

At least once a week

In year 2 of PhD study

At least once a week

In year 3 of PhD study

At least once a week

These meetings will be a mixture of face to face and via video chat, whatever is preferred/convenient. I am usually contactable for an instant response on every working day.

Working Pattern

The timing of work is completely flexible, apart from the need to attend pre-arranged meetings. The PhD student can work 9 am-5 pm or work outside of core hours, but more support will be available in core hours.

Notice Period for Feedback

I need at least 1 week’s notice to provide feedback on written work of up to 5000 words.

MIBTP Project Details

Primary supervisor for:

Exploring the structure and mechanisms of non-canonical microbial mechanosensitive channels

See the PhD Opportunities section to see if this project is currently open for applications via MIBTP.

Please Note: The main page lists projects via BBSRC Research Theme(s) quoted and then relevant Topic(s)

Exploring the structure and mechanisms of non-canonical microbial mechanosensitive channels

Secondary Supervisor(s): Dr Emma Hesketh, Professor Alan Goddard

University of Registration: Aston University

BBSRC Research Themes:

Understanding the Rules of Life (Microbiology, Structural Biology,)

Project Outline

Membrane proteins have evolved alongside lipid molecules, and their structure and function are altered by the chemical and physical properties of the bilayer. For mechanosensitive channels, this protein-lipid relationship is even more intimate, as these systems sense and respond to bilayer tension changes. In E. coli, seven mechanosensitive channels have been identified. These channels sense increases in membrane tension generated during hypoosmotic shock, allowing bacteria to release solutes to prevent cell lysis. However, their redundancy implies other physiological roles, and several have been implicated in pathogenicity and are potential microbial targets.

In other microbes, mechanosensitive channels can have additional domains potentially enabling regulation or crosstalk with other cellular responses. These non-canonical channels retain the conserved mechanosensitive channel core but are fused to additional sensory or regulatory domains. Their architectures raise the possibility that mechanical signals are integrated with chemical and metabolic cues, allowing mechanosensitive channels to participate in signalling pathways beyond their role in osmotic protection.

This project will investigate how additional domains regulate the mechanosensitive channel core and how signals such as ligand binding and membrane interactions alter channel structure and function. By determining structures of these channels in different states, we will uncover how these proteins integrate mechanical and chemical signals. Comparing diverse domain architectures will reveal how sensory functions evolve around a conserved membrane protein scaffold, providing insights into mechanosensation and membrane protein evolution. The project will benefit from excellent facilities at the Aston Institute for Membrane Excellence, which provides infrastructure for the production and analysis of membrane proteins, and state-of-the-art cryoEM infrastructure at the Midlands Regional CryoEM Facility.