LAT--an important raft-associated transmembrane adaptor protein. Delivered on 6 July 2009 at the 34th FEBS Congress in Prague, Czech Republic
Language English Country England, Great Britain Media print-electronic
Document type Lecture, Research Support, Non-U.S. Gov't
- MeSH
- Adaptor Proteins, Signal Transducing genetics metabolism MeSH
- Models, Biological MeSH
- Humans MeSH
- Membrane Microdomains metabolism MeSH
- Membrane Proteins genetics metabolism MeSH
- Mutation MeSH
- Receptors, Antigen, T-Cell metabolism MeSH
- Receptors, Cell Surface metabolism MeSH
- Signal Transduction * MeSH
- Protein Binding MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Research Support, Non-U.S. Gov't MeSH
- Lecture MeSH
- Names of Substances
- Adaptor Proteins, Signal Transducing MeSH
- LAT protein, human MeSH Browser
- Membrane Proteins MeSH
- Receptors, Antigen, T-Cell MeSH
- Receptors, Cell Surface MeSH
Membrane rafts are microdomains involved in a number of biologically important processes, including immunoreceptor signalling. Among the functionally important protein components of these microdomains are transmembrane adaptor proteins, containing in their intracellular domains tyrosine residues that can be phosphorylated and bind other cytoplasmic signalling proteins. The most important leukocyte transmembrane adaptor protein is LAT (linker for activation of T cells), which is critically involved in T cell receptor signalling, but also plays important roles in signal initiation by several other immunologically important receptors. Here we review recent progress in the elucidation of several aspects of this protein, e.g. the controversy concerning the importance of LAT being present in membrane rafts, the involvement in signalling through a number of receptors other than the T cell receptor and the puzzling phenotype of some LAT mutants.
References provided by Crossref.org
Lck, Membrane Microdomains, and TCR Triggering Machinery: Defining the New Rules of Engagement