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A Novel Function of Karyopherin β3 Associated with Apolipoprotein A-I Secretion  

Chung, Kyung Min (Department of Microbiology and Immunology, Chonbuk National University Medical School)
Cha, Sun-Shin (Marine Biotechnology Center, Korea Ocean Research and Development Institute)
Jang, Sung Key (Department of Life Science, Division of Molecular and Life Sciences, Pohang University of Science and Technology)
Abstract
Human karyopherin ${\beta}3$, highly homologous to a yeast protein secretion enhancer (PSE1), has often been reported to be associated with a mediator of a nucleocytoplasmic transport pathway. Previously, we showed that karyopherin ${\beta}3$ complemented the PSE1 and KAP123 double mutant. Our research suggested that karyopherin beta has an evolutionary function similar to that of yeast PSE1 and/or KAP 123. In this study, we performed yeast two-hybrid screening to find a protein which would interact with karyopherin ${\beta}3$ and identified apolipoprotein A-I (apo A-I), a secretion protein with a primary function in cholesterol transport. By using in vitro binding assay, co-immunoprecipitation, and colocalization studies, we defined an interaction between karyopherin ${\beta}3$ and apo A-I. In addition, overexpression of karyopherin ${\beta}3$ significantly increased apo A-I secretion. These results suggest that karyopherin ${\beta}3$ plays a crucial role in apo A-I secretion. These findings may be relevant to the study of a novel function of karyopherin ${\beta}3$ and coronary artery diseases associated with apo A-I.
Keywords
apolipoprotein A-I; coronary artery diseases; karyopherin ${\beta}3$; PSE1; secretion enhancer;
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