FYVE Domain

The FYVE domain is a phosphatidylinositol-3-phosphate-binding module of approximately 60 to 80 amino acids. It was named after the first four proteins, where this domain was described (Fablp, YOTB, Vaclp and EEA1). 

FYVE Domain Fz Receptors G-actin G-Proteins GABA... 

Misra, S. and J. H. Hurley, Crystal structure of a phosphatidylinositol 3-phosphate-specific membranetargeting motif, the FYVE domain of Vps27p. Cell, 1999, 97(5), 657-66. 

Tsukazaki, T., et al., SARA, a FYVE domain protein that recruits Smad2 to... 

Tsukazaki, T., Chiang, T.A., Davison, A.F., Attisano, L., and Wrana, J.L. 1998. SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor. Cell 95 779-791. 

Wurmser, A.E., Gary, J.D. and Emr, S.D., 1999, Phosphoinositide 3-kinases and their FYVE domain-containing effectors as regulators of vacuolar/lysosomal membrane trafficking pathways. J. Biol. Chem. 274 9129-9132. 

Membrane-targeting Domains Pleckstrin Homology (PH) Domains and FYVE Domains PH Domains... 

The FYVE domain is a cysteine-rich domain which binds two zinc ions and has binding specificity for PtdIns(3)P, one of the membrane-localized products of the PI3-ki-nase reaction (see Chapter 6). Proteins containing FYVE domains have been implicated, e. g., in membrane trafficking and in signaling by Smad proteins (review Gil-looly et al., 2001). It is assumed that binding of FYVE domain-containing proteins to PtdIns(3)P mediates their membrane association. 

Gillooly, D.J., Simonsen, A. and Stenmark, H. (2001) Cellular functions of phosphati-dylinositol 3-phosphate and FYVE domain proteins. Biochem.J., 355, 249-258. 

Computer Modeling of the Membrane Interaction of FYVE Domains. 

Solution structure of a trypanosomatid FYVE domain- proteins that play key roles in regulating membrane traffic in eukaryotic cells. 

Here, our membrane protein is the FYVE domain (which is named for its identification with four proteins (Fablip, YOTB, Vaclp, EEAI) and the ligand is Ptdlns(3)P, an abbreviation for phosphatidylinositole-3-phosphate. 

Figure 19.18 shows (a) the structure of the protein of EEAI in the FYVE domain, (b) the phosphate group in Ptdlns(3)P recognition by arginines, and (c) interactions in the Ptdlns(3)P pocket. 

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