Disease relevance of BOI1

• Interaction selection by biopanning from a fragmented yeast proteome displayed on filamentous phage particles was successful in identifying proline-rich fragments of Boi1p and Boi2p [1].

High impact information on BOI1

• A BOI2 homologue, BOI1, was identified as a gene whose overexpression inhibited cell growth [2].
• Deletion of BOI1 and BO12 together leads to impaired morphogenesis and poor ability [3].
• Consistent with these possibilities, overexpression of Boi1p inhibits bud emergence, but this inhibition is counteracted by cooverexpression of Cdc42p [3].
• Here, we present evidence that through its second SH3 domain, Bem1p binds to the structurally and functionally similar proteins Boi1p and Boi2p, each of which contain an SH3 and pleckstrin homology (PH) domain [3].
• Overexpression of the BNI1 deltaN and BOI1 deltaN genes, which lacked amino-terminal sequences, was associated with phenotypes similar to those of mutants defective in bud formation [4].

Biological context of BOI1

• Amino-acid substitutions that diminish binding to PIP2 and PS impair Boi1 function [5].
• Boi1 and Boi2 are localized to the periphery of buds during much of the budding cycle and to necks late in the cell cycle [5].

Other interactions of BOI1

• A PH domain-bearing segment of Boi1p that lacks the Bem1p-binding site is necessary and sufficient for function [3].
• Pob1p is homologous to two functionally redundant Saccharomyces cerevisiae proteins, Boi1p and Boi2p, which are necessary for cell growth and relevant to bud formation [6].

References