By R. J. Botelho, C. C. Scott, S. Grinstein (auth.), Professor Harald Stenmark (eds.)
The reversible recruitment of intracellular protein complexes to membranes is vital for immune phone capabilities, together with chemotaxis, phagocytosis and signalling. Such recruitment is frequently managed by way of phosphorylated derivatives of phosphatidylinositol, often called phosphoinositides. those lipids additionally serve to turn on enzyme structures that perform advanced reactions akin to chromatin remodelling and pre-mRNA procesing. This factor of present subject matters in Microbiology and Immunology offers an summary of ways phosphoinositides functionality in protein recruitment and enzyme activation and offers physiologically very important examples of protein-phosphoinositide interactions.
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Additional info for Phosphoinositides in Subcellular Targeting and Enzyme Activation
Sample text
2001), whereas almost all of the other PX domains bind specifically to PtdIns3P. The role of the PX domain in PI3K C2ais not yet clear, although it may recruit the kinase to areas rich in PtdIns(4,S)P 2 where other endocytic proteins are also concentrated. Therefore, PI3K C2amay be activated directly by clathrin to convert PtdIns(4,S)P 2 effectively into PtdIns(3,4,S)P 3 and thus may rearrange the endocytic complex. 4 ENTH Domains as PtdIns(4,S)P 2 Targets Essential for Endocytosis A protein bound to Eps1S was identified and referred to as epsin (Chen et al.
38 5 Structural Basis of Phosphoinositide-ENTH Interactions . . . . 40 6 Conclusions and Perspectives . . . . . . . . . . . . . 42 References. . . . . . . . . . . . . . . . . . . . 43 Abstract Clathrin-mediated endocytosis starts by a recruitment of endocytic proteins to the plasma membrane to induce invagination of lipid bilayer and subsequent vesicule formation. The recruitment of these components requires Ptdlns(4,5)Pz, a phosphoinositide on the plasma membrane.
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