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- W2040604420 endingPage "140" @default.
- W2040604420 startingPage "115" @default.
- W2040604420 abstract "This chapter discusses the structural basis of a specialized zinc finger that binds PtdIns 3-phosphate [PI(3)P], termed the FYVE domain, and the roles played by several proteins harboring this motif in membrane trafficking and cell signaling. The recruitment of cytoplasmic proteins to specific membrane compartments is important for a diverse spectrum of cellular processes including intracellular protein trafficking, cytokine and growth factor receptor signaling, actin cytoskeleton organization and apoptosis. The identification of the FYVE domain as a specific PI(3)P binding motif has significantly impacted the field of membrane trafficking and shed light on additional cellular functions of PI(3)P. Through localization studies of the FYVE domain using both conventional light microscopy and high resolution electron microscopy, PI(3)P has been found to exist in endosomal membranes, on intralumenal vesicles contained within MVBs, autophagosomes, and in vacuolar/lysosomal membranes. Recent studies indicate that another lipid binding motif, the PX domain, specifically recognizes PI(3)P. Further studies are required to determine the validity of this concept and whether this is a general principle or may only apply to a certain subset of FYVE-domain containing proteins." @default.
- W2040604420 created "2016-06-24" @default.
- W2040604420 creator A5078013249 @default.
- W2040604420 date "1981-11-01" @default.
- W2040604420 modified "2023-10-13" @default.
- W2040604420 title "Phosphatidyldmositol hydrolysis: A multifunctional transducing mechanism" @default.
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