| Literature DB >> 12606027 |
Sidonie Wicky1, Sabine Frischmuth, Birgit Singer-Krüger.
Abstract
In this study we identified a novel protein, Bsp1p, that interacts directly with two yeast synaptojanins, Sjl2p and Sjl3p, but not with Sjl1p. The interaction takes place via the Sac1/polyphosphoinositide phosphatase domain, whose conserved C-terminal region is important for binding. Subcellular localization and genetic interactions revealed a function of Bsp1p in the cortical actin cytoskeleton. A fraction of Bsp1p was found to be membrane-associated. Studies with mutants of phosphatidylinositol 4-kinase, PIK1, suggested that the interaction with membranes is facilitated by phosphoinositides. We propose that Bsp1p is an adapter that links Sjl2p and Sjl3p to the cortical actin cytoskeleton.Entities:
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Year: 2003 PMID: 12606027 DOI: 10.1016/s0014-5793(03)00067-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124