Ser-Phosphorylation of PCSK9 (Proprotein Convertase Subtilisin-Kexin 9) by Fam20C (Family With Sequence Similarity 20, Member C) Kinase Enhances Its Ability to Degrade the LDLR (Low-Density Lipoprotein Receptor)

Author:

Ben Djoudi Ouadda Ali1,Gauthier Marie-Soleil2,Susan-Resiga Delia1,Girard Emmanuelle1,Essalmani Rachid1,Black Miles3,Marcinkiewicz Jadwiga1,Forget Diane2,Hamelin Josée1,Evagelidis Alexandra1,Ly Kevin4,Day Robert4,Galarneau Luc5,Corbin Francois5,Coulombe Benoit2,Çaku Artuela5,Tagliabracci Vincent S.3,Seidah Nabil G.1

Affiliation:

1. From the Laboratory of Biochemical Neuroendocrinology, Montreal Clinical Research Institute (IRCM; affiliated to the Université de Montréal), QC, Canada (A.B.D.O., D.S.-R., E.G., R.E., J.M., J.H., A.E., N.G.S.)

2. Translational Proteomics Research Unit, Clinical Research Institute of Montreal (IRCM, affiliated to the Université de Montréal), QC, Canada (M.-S.G., D.F., B.C.)

3. Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas (M.B., V.S.T.)

4. Institut de Pharmacologie, Université de Sherbrooke, QC, Canada (K.L., R.D.)

5. Department of Biochemistry, Université de Sherbrooke, and Centre de Recherche du CHUS, QC, Canada (L.G., F.C., A.Ç.).

Abstract

Objective: PCSK9 (proprotein convertase subtilisin-kexin 9) enhances the degradation of the LDLR (low-density lipoprotein receptor) in endosomes/lysosomes. This study aimed to determine the sites of PCSK9 phosphorylation at Ser-residues and the consequences of such posttranslational modification on the secretion and activity of PCSK9 on the LDLR. Approach and Results: Fam20C (family with sequence similarity 20, member C) phosphorylates serines in secretory proteins containing the motif S-X-E/phospho-Ser, including the cholesterol-regulating PCSK9. In situ hybridization of Fam20C mRNA during development and in adult mice revealed a wide tissue distribution, including liver, but not small intestine. Here, we show that Fam20C phosphorylates PCSK9 at Serines 47, 666, 668, and 688. In hepatocytes, phosphorylation enhances PCSK9 secretion and maximizes its induced degradation of the LDLR via the extracellular and intracellular pathways. Replacing any of the 4 Ser by the phosphomimetic Glu or Asp enhanced PCSK9 activity only when the other sites are phosphorylated, whereas Ala substitutions reduced it, as evidenced by Western blotting, Elisa, and LDLR-immunolabeling. This newly uncovered PCSK9/LDLR regulation mechanism refines our understanding of the implication of global PCSK9 phosphorylation in the modulation of LDL-cholesterol and rationalizes the consequence of natural mutations, for example, S668R and E670G. Finally, the relationship of Ser-phosphorylation to the implication of PCSK9 in regulating LDL-cholesterol in the neurological Fragile X-syndrome disorder was investigated. Conclusions: Ser-phosphorylation of PCSK9 maximizes both its secretion and activity on the LDLR. Mass spectrometric approaches to measure such modifications were developed and applied to quantify the levels of bioactive PCSK9 in human plasma under normal and pathological conditions.

Publisher

Ovid Technologies (Wolters Kluwer Health)

Subject

Cardiology and Cardiovascular Medicine

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3