Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site.

摘要: Summary F-BAR domains control membrane interactions in endocytosis, cytokinesis, and cell signaling. Although they are generally thought to bind curved membranes containing negatively charged phospholipids, numerous functional studies argue that differences in lipid-binding selectivities of functionally important. Here, we compare membrane-binding properties the Saccharomyces cerevisiae in vitro in vivo. Whereas some (such as Bzz1p Hof1p F-BARs) equally well all domain from RhoGAP Rgd1p preferentially binds phosphoinositides. We determined X-ray crystal structures Rgd1p, latter bound an inositol phosphate. The explain phospholipid-binding selectivity reveal phosphoinositide binding site is fully conserved a mammalian called Gmip partly retained certain other domains. Our findings previously unappreciated determinants specificity provide basis for its prediction sequence.