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. Author manuscript; available in PMC: 2007 Oct 5.
Published in final edited form as: Biochim Biophys Acta. 2007 Apr 12;1771(6):727–736. doi: 10.1016/j.bbalip.2007.04.002

Figure 3. An intermembrane contact site model for SFH protein function.

Figure 3

(A) SFH proteins (grey) may themselves be integral components of intermembrane contact sites, employing their intrinsic PtdIns-binding capacity (in black) to traffic PtdIns through a portal. (B) An SFH protein may employ its ability to present PtdIns to a phosphoinositide kinase to generate a phosphoinositide platform that recruits intrinsic component(s) (Factor X) of an intermembrane contact site. In this scenario, the SFH protein does not directly utilize its PtdIns-binding properties to impose PtdIns-trafficking specificity through such a site. Other lipid species could pass through such a site. This model most likely applies to the case of Sfh4p-dependent trafficking of PtdSer to an extramitochondrial PtdSer decarboxylase [55; see text].