Digitale Medien
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Biophysics and Biomolecular Structure
29 (2000), S. 49-79
ISSN:
1056-8700
Quelle:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Thema:
Biologie
,
Physik
Notizen:
Abstract Protein kinase C homology-1 and -2, FYVE, and pleckstrin homology domains are ubiquitous in eukaryotic signal transduction and membrane-trafficking proteins. These domains regulate subcellular localization and protein function by binding to lipid ligands embedded in cell membranes. Structural and biochemical analysis of these domains has shown that their molecular mechanisms of membrane binding depend on a combination of specific and nonspecific interactions with membrane lipids. In vivo studies of green fluorescent protein fusions have highlighted the key roles of these domains in regulating protein localization to plasma and internal membranes in cells.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1146/annurev.biophys.29.1.49
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