Structural properties of lipid-binding sites in cytoskeletal proteins.

V Niggli

Journal: Trends in biochemical sciences 2001;26(10):604-11

PMID: 11590013

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Abstract

Several cytoskeletal proteins have been shown to interact in vitro with, and in some cases are regulated by, specific membrane lipids. In some cases, evidence for in situ interactions has been provided. The molecular basis for such interactions is now being unravelled. At least five structurally distinct types of lipid-binding sites in cytoskeletal proteins have been identified. However, our understanding of the physiological role of such interactions is still limited. Precise knowledge about the binding-site structures and the actual amino acid residues involved should now enable the expression of mutant proteins that specifically lack the ability to interact with lipids. The impact of these mutations on protein location and function can then be assessed.

Address: Dept of Pathology, University of Bern, Murtenstrasse 31, CH-3010 Bern, Switzerland. [email protected]

DOI: 10.1016/s0968-0004(01)01927-2

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MeSH Terms: Annexins, Binding Sites, Blood Proteins, Contractile Proteins, Cytoskeletal Proteins, Dynamins, GTP Phosphohydrolases, Gelsolin, In Vitro Techniques, Intracellular Signaling Peptides and Proteins, Lipid Metabolism, Membrane Microdomains, Membrane Proteins, Microfilament Proteins, Models, Molecular, Myristoylated Alanine-Rich C Kinase Substrate, Phosphoproteins, Profilins, Protein Structure, Tertiary, Proteins, Signal Transduction, Spectrin, Vinculin