1. PI4KII activity-dependent Golgi complex targeting of Aplysia phosphodiesterase 4 long-form mutant
- Author
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Jin-A Lee, Bong-Kiun Kaang, Yong-Woo Jun, and Deok-Jin Jang
- Subjects
0301 basic medicine ,Phosphatidylinositol 4-phosphate ,Mutant ,Phosphodiesterase ,Antimycin A ,Biology ,Golgi apparatus ,General Biochemistry, Genetics and Molecular Biology ,Cell biology ,Wortmannin ,03 medical and health sciences ,chemistry.chemical_compound ,symbols.namesake ,030104 developmental biology ,chemistry ,Biochemistry ,symbols ,Animal Science and Zoology ,Phenylarsine oxide ,Phosphatidylinositol - 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 h...
- Published
- 2017