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The spectrin family - proteins with many structural and functional roles in the cell

Research project My research group has a long-standing interest in spectrin and spectrin-like proteins, such as α-actinin. The major aim is to understand the structural and functional roles of these proteins.

My research group has a long-standing interest in spectrin and spectrin-like proteins. The major aim is to understand the structural and functional roles of these proteins. Presently our efforts are focused on two different areas: to determine the structure and dynamics of a spectrin repeat by NMR and to characterise α-actinin from Entamoeba and S pombe.

Head of project

Lars Backman
Professor, senior
E-mail
Email

Project overview

Project period

2018-01-11 2020-12-31

Funding

EU, 2003-2004: SEK 1,200,000

Research subject

Biological sciences, Chemical sciences, Molecular biology and genetics

Project description

The proteins of the spectrin-based membrane skeleton are members of closely related gene families with widespread distribution. Although the basic structural role established in red cells is likely to apply in nonerythroid tissue, the regulation of gene expression, the structure in terms of protein-protein interactions and function are considerably more diverse.
The network links to both lipid and protein components of membranes. The proteins are diverse and include cell adhesion molcecules, ion transporters, channels, receptors, enzymes and others. Such a diversity of biological roles means that membrane skeleton proteins link with many diseases. However, their organisation and function are not well characterised owing to the diversity of genes and extensive alternative splicing.
Before we can understand the variety of functions the membrane skeleton fulfils at multiple sites in nonerythroid cells, we need a better knowledge of spectrin as well as of proteins that interact with spectrin.
We propose therefore to use biochemical and molecular biology techniques, in particular CD and fluorescence spectroscopy and 2D electrophoresis combined with mass spectroscopy and two-hybrid screening to further the knowledge of spectrin and its cellular function.
Specific goals include to determine the structure and specificity of the SH3 and C terminal domains, two important structural domains of spectrin and to identify proteins that interact with these domains.