کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2131457 1086643 2009 12 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Basal endothelial nitric oxide synthase (eNOS) phosphorylation on Ser1177 occurs in a stable microtubule- and tubulin acetylation-dependent manner
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی تحقیقات سرطان
پیش نمایش صفحه اول مقاله
Basal endothelial nitric oxide synthase (eNOS) phosphorylation on Ser1177 occurs in a stable microtubule- and tubulin acetylation-dependent manner
چکیده انگلیسی

To better understand the relationship between the subcellular compartmentalization of endothelial nitric oxide synthase (eNOS) and its function in endothelial cells, we addressed the roles of the microtubule network and of its dynamics in organizing Golgi-bound eNOS. We found that part of Golgi-bound eNOS localizes to the trans-Golgi network and/or to trans-Golgi network-derived vesicles and membrane tubules that are organized preferentially by stable microtubules. Also, while most of cellular eNOS was recovered in a detergent-resistant microtubule-enriched subcellular fraction, its recovery was impaired after total microtubule disassembly, but not after selective disassembly of dynamic microtubules or after microtubule stabilization. Basal eNOS phosphorylation on Ser1177 further required the association of the trans-Golgi network to stable microtubules and was enhanced by microtubule stabilization. We finally show that the involvement of stable microtubules in basal eNOS phosphorylation involved alpha-tubulin acetylation. Microtubule-dependent organization of subcellular eNOS and control over its phosphorylation would thus be essential for endothelial cells to maintain their basal eNOS function.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 315, Issue 20, 10 December 2009, Pages 3509–3520
نویسندگان
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