Basal endothelial nitric oxide synthase (eNOS) phosphorylation on Ser1177 occurs in a stable microtubule- and tubulin acetylation-dependent manner

被引：16

作者：

Giustiniani, J. ^{[1
]}

Couloubaly, S. ^{[2
]}

Baillet, A. ^{[1
]}

Pourci, M-L. ^{[2
,3
]}

Cantaloube, I. ^{[1
]}

Fourniat, C. ^{[2
]}

Paul, J-L. ^{[2
,4
]}

Poues, C. ^{[1
,5
]}

机构：

[1] Univ Paris 11, Fac Pharm, Lab Biochim & Biol Cellulaire, JE 2493,IFR141, F-92290 Chatenay Malabry, France

[2] Univ Paris 11, Fac Pharm, Lab Physiol & Biochim Appl, INRA UMR 1154,IFR141, F-92290 Chatenay Malabry, France

[3] Hop Bicetre, APHP, Biochim Lab, Le Kremlin Bicetre, France

[4] Hop Europeen Georges Pompidou, APHP, Biochim Lab, F-75015 Paris, France

[5] Hop Antoine Beclere, APHP, Lab Biochim Hormonol, Clamart, France

来源：

EXPERIMENTAL CELL RESEARCH | 2009年 / 315卷 / 20期

关键词：

Endothelial nitric oxide synthase; trans-Golgi network; Microtubules; Tubulin acetylation; PROTEIN-KINASE; GROWTH-FACTOR; NO SYNTHASE; CELL-DEATH; IN-VITRO; GOLGI; INHIBITION; CAVEOLIN; PATHWAY; BINDING;

D O I：

10.1016/j.yexcr.2009.07.018

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

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 Ser(1177) 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. (C) 2009 Published by Elsevier Inc.

引用

页码：3509 / 3520

页数：12

共 62 条

[31] Dephosphorylation of endothelial nitric-oxide synthase by vascular endothelial growth factor - Implications for the vascular responses to cyclosporin A [J].