Probing the importance and potential roles of the binding of the PH-domain protein Boi1 to acidic phospholipids.

ABSTRACT:

Background

The related proteins Boi1 and Boi2, which appear to promote polarized growth in S. cerevisiae, both contain a PH (pleckstrin homology) and an SH3 (src homology 3) domain. Previously, we gained evidence that a PH domain-bearing segment of Boi1, which we call Boi1-PH, is sufficient and necessary for function. In the current study, we investigate the binding of Boi1's PH domain to the acidic phospholipids PIP2 (phosphatidylinositol-4,5-bisphosphate) and PS (phosphatidylserine).

Results

Boi1-PH co-sediments with PS vesicles. It does so more readily when these vesicles contain a small amount of PIP2. Boi1-PH is degraded in yeast extracts in a manner that is stimulated by PIP2. Amino-acid substitutions that diminish binding to PIP2 and PS impair Boi1 function. Fusion to

SUBMITTER: Hallett MA 

PROVIDER: S-EPMC117597 | biostudies-literature | 2002 Jun

REPOSITORIES: biostudies-literature