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. Author manuscript; available in PMC: 2010 Jul 25.
Published in final edited form as: Proteins. 2009 Sep;76(4):852–860. doi: 10.1002/prot.22392

Figure 3.

Figure 3

The pH-sensitivity is a general feature of the FYVE domain family. (a) The SDS-PAGE gels show the partition of Hrs1, RUFY1, Vps27p, and WDFY1 FYVE domains between the supernatant (s) and PtdIns(3)P-enriched liposome pellet (p) at different pHs. (b) Changes in localization of EGFP-tagged RUFY1, Vps27p, and WDFY1 FYVE domains in HeLa cells upon varying the cytosolic pH. The cells were incubated in solutions buffered to indicated pH prior to visualizing by fluorescence microscopy. (c) The tandem His residues are conserved in the FYVE domain family. Alignment of the FYVE domain sequences: absolutely, moderately, and weakly conserved residues are colored brown, orange, and yellow, respectively. The His residues are in green. Three regions of the FYVE domain involved in coordination of PtdIns(3)P are indicated by black lines above the alignment. (d) The PtdIns(3)P binding pocket defined from the crystal structures of Vps27p FYVE (PDB 1VFY), EEA1 FYVE (PDB 1JOC), and Hrs FYVE (PBD 1DVP). The tandem His residues and Arg/Lys residues located in the R(R/K)HHCRXCG and RVC regions are labeled and colored green and dark gray, respectively.