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Mol. Cells 2008; 26(3): 291-298

Published online September 30, 2008

© The Korean Society for Molecular and Cellular Biology

A Novel Function of Karyopherin Beta3 Associated with Apolipoprotein A-I Secretion

Kyung Min Chung, Sun-Shin Cha and Sung Key Jang

Abstract

Human karyopherin beta3, 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 beta3 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 beta3 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 ?3 and apo A-I. In addition, overexpression of karyopherin ?3 significantly increased apo A-I secretion. These results suggest that karyopherin beta3 plays a crucial role in apo A-I secretion. These findings may be relevant to the study of a novel function of karyopherin beta3 and coronary artery diseases associated with apo A-I.

Keywords coronary artery diseases, secretion enhancer, apolipoprotein A-I, karyopherin β3, PSE1

Article

Research Article

Mol. Cells 2008; 26(3): 291-298

Published online September 30, 2008

Copyright © The Korean Society for Molecular and Cellular Biology.

A Novel Function of Karyopherin Beta3 Associated with Apolipoprotein A-I Secretion

Kyung Min Chung, Sun-Shin Cha and Sung Key Jang

Abstract

Human karyopherin beta3, 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 beta3 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 beta3 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 ?3 and apo A-I. In addition, overexpression of karyopherin ?3 significantly increased apo A-I secretion. These results suggest that karyopherin beta3 plays a crucial role in apo A-I secretion. These findings may be relevant to the study of a novel function of karyopherin beta3 and coronary artery diseases associated with apo A-I.

Keywords: coronary artery diseases, secretion enhancer, apolipoprotein A-I, karyopherin β3, PSE1

Mol. Cells
Jan 31, 2023 Vol.46 No.1, pp. 1~67
COVER PICTURE
RNAs form diverse shapes and play multiple functions as central molecules of gene expression. In this special issue on RNA, seven minireviews illustrate how basic concepts and recent RNA biology findings are transformed into new and exciting RNA therapeutics.

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