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PI4KII activity-dependent Golgi complex targeting of Aplysia phosphodiesterase 4 long-form mutant

Animal Cells and Systems 2017년 21권 5호 p.316 ~ 322
전용우, 이진아, 강봉균, 장덕진,
소속 상세정보
전용우 ( Jun Yong-Woo ) - Kyungpook National University College of Ecology and Environment Department of Ecological Science
이진아 ( Lee Jin-A ) - Hannam University College of Life Science and Nanotechnology Department of Biological Sciences and Biotechnology
강봉균 ( Kaang Bong-Kiun ) - Seoul National University College of Natural Sciences Department of Biological Sciences
장덕진 ( Jang Deok-Jin ) - Kyungpook National University College of Ecology and Environment Department of Ecological Science

Abstract


The compartmentalization of cAMP by specifically targeted phosphodiesterases (PDEs) contributes to signal regulation in defined regions of cells. We previously demonstrated that the 20 N-terminal amino acids of Aplysia PDE4 (ApPDE4) long-form (L(N20)) and the two mutants of L(N20) were localized to the Golgi complex. However, the molecular mechanisms underlying the Golgi complex targeting of ApPDE4 long-form and its mutated forms are not clear. In the present study, we show that the Golgi complex targeting of L(N20/C14,15S)-enhanced green fluorescent protein (EGFP) was antimycin A-, phenylarsine oxide (PAO)-, and adenosine-sensitive, but insensitive to high concentrations of wortmannin. On the other hand, the Golgi complex targeting of L(N20)-EGFP and L(N20/C3,14S)-EGFP was antimycin A- and PAO-insensitive. These results suggest that the Golgi-localized lipid kinase protein, phosphatidylinositol 4-kinase type II alpha (PI4KIIα), the activity of which is inhibited by PAO and adenosine, but not by high concentrations of wortmannin, is likely involved in the Golgi complex targeting of L(N20/C14,15S)-EGFP. In addition, subcellular localization of L(N20/C14,15S)-EGFP, but not L(N20)-EGFP or L(N20/C3,14S)-EGFP, was changed from the Golgi complex only to both the endoplasmic reticulum (ER) and the Golgi complex following treatment with a palmitoylation inhibitor, 2-bromo palmitate. Taken together, our results suggest that L(N20/C14,15S)-EGFP, but not L(N20)-EGFP or L(N20/C3,14S)-EGFP, is localized to the Golgi complex in a PI4KII activity- and palmitoylation-dependent manner. Therefore, phosphatidylinositol 4-phosphate (PI4P) generated by PI4KIIα at the Golgi complex might play a key role in the Golgi complex targeting of L(N20/C14,15S)-EGFP.

키워드

Aplysia; phosphodiesterase 4; Golgi complex; phosphatidylinositol 4-phosphate; phosphatidylinositol 4-kinase type II alpha

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