Binding of Phosphatidylinositol-3 ,4,5 -Triphosphate to 45-kDa Sec14-like Protein from the Rat Olfactory Epithelium in Liposomes

E. V. Il'nitskaya , # O. G. Shamborant , V. V. Radchenko , T. M. Shuvaeva , and V. M. Lipkin

# Phone: +7 (495) 335-5511, fax: +7 (495) 335-0812, e-mail: shuvaeva@mail.ibch.ru

Shemyakin -- Ovchinnikov Institute of Bioorganic Chemistry , Russian Academy of Sciences , ul . Miklukho-Maklaya 16/10, Moscow , 117997 Russia

Received December 26, 2005; in final form, December 30, 2005

Abstract: The binding of phosphatidylinositol-3,4,5-triphosphate to a protein with molecular mass of 45 kDa from rat olfactory epithelium (p45) was investigated using a model membrane system. Liposomes containing a mixture of phospholipids (phosphatidylethanolamine, phosphatidylcholine, and phosphatidylinositol-3,4,5-triphosphate) were used in the study. The binding of the protein to liposomes caused by its interaction with phosphatidylinositol-3,4,5-triphosphate was confirmed by cosedimentation and immunoblotting with chemiluminescent detection using monoclonal antibodies to the native protein p45.

Key words: cosedimentation , CRAL/TRIO-domain, liposomes , 45, phosphatidylinositol-3 ,4,5 -triphosphate, Sec14-like proteins

Russian Journal of Bioorganic Chemistry 2006, 32 (3):301-302