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Stepwise processing analyses of the single-turnover PCSK9 protease reveal its substrate sequence specificity and link clinical genotype to lipid phenotype

Chorba, John S., Galvan, Adri M., Shokat, Kevan M.·2018·Journal of Biological Chemistry
DOI 10.1074/jbc.ra117.000754
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  • Both loss-of-function and gain-of-function PCSK9 mutations can impair PCSK9 secretion and reduce its plasma levels.

    “However, both loss-of-function and gain-of-function mutations can impair PCSK9 secretion and reduce its plasma levels34–38.”

    From Membrane type 1 matrix metalloproteinase promotes LDL receptor shedding and accelerates the development of atherosclerosis (2021) · cites this paper as [35]

    The secretion-assay section reports that most PCSK9 mutants affecting secretion reduced it, and the Discussion specifically describes impaired secretion for S127R, a gain-of-function mutant. The paper does not establish that these secretion defects reduce plasma PCSK9 levels; its Discussion instead notes that serum levels fluctuate substantially. (LLM, conf=0.87)

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  1. Park, 2004, Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver, J. Biol. Chem, 279, 50630, 10.1074/jbc.M410077200 · DOI · Paper page
  2. Maxwell, 2005, Overexpression of PCSK9 accelerates the degradation of the LDLR in a post-endoplasmic reticulum compartment, Proc. Natl. Acad. Sci. U.S.A, 102, 2069, 10.1073/pnas.0409736102 · DOI · Paper page
  3. Zhang, 2007, Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation, J. Biol. Chem, 282, 18602, 10.1074/jbc.M702027200 · DOI · Paper page
  4. Grefhorst, 2008, Plasma PCSK9 preferentially reduces liver LDL receptors in mice, J. Lipid Res, 49, 1303, 10.1194/jlr.M800027-JLR200 · DOI · Paper page
  5. Seidah, 2016, New developments in proprotein convertase subtilisin–kexin 9's biology and clinical implications, Curr. Opin. Lipidol, 27, 274, 10.1097/MOL.0000000000000295 · DOI · Paper page
  6. Cohen, 2006, Sequence variations in PCSK9, low LDL, and protection against coronary heart disease, N. Engl. J. Med, 354, 1264, 10.1056/NEJMoa054013 · DOI · Paper page
  7. Maxwell, 2004, Adenoviral-mediated expression of Pcsk9 in mice results in a low-density lipoprotein receptor knockout phenotype, Proc. Natl. Acad. Sci. U.S.A, 101, 7100, 10.1073/pnas.0402133101 · DOI · Paper page
  8. Naureckiene, 2003, Functional characterization of Narc 1, a novel proteinase related to proteinase K, Arch. Biochem. Biophys, 420, 55, 10.1016/j.abb.2003.09.011 · DOI
  9. Seidah, 2012, The biology and therapeutic targeting of the proprotein convertases, Nat. Rev. Drug Discov, 11, 367, 10.1038/nrd3699 · DOI · Paper page
  10. Cunningham, 2007, Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia, Nat. Struct. Mol. Biol, 14, 413, 10.1038/nsmb1235 · DOI · Paper page
  11. Mayne, 2011, Novel loss-of-function PCSK9 variant is associated with low plasma LDL cholesterol in a French-Canadian family and with impaired processing and secretion in cell culture, Clin. Chem, 57, 1415, 10.1373/clinchem.2011.165191 · DOI · Paper page
  12. Piper, 2007, The crystal structure of PCSK9: a regulator of plasma LDL-cholesterol, Structure, 15, 545, 10.1016/j.str.2007.04.004 · DOI · Paper page
  13. Hampton, 2007, The self-inhibited structure of full-length PCSK9 at 1.9 Å reveals structural homology with resistin within the C-terminal domain, Proc. Natl. Acad. Sci. U.S.A, 104, 14604, 10.1073/pnas.0703402104 · DOI
  14. Chorba, 2014, The proprotein convertase subtilisin/kexin type 9 (PCSK9) active site and cleavage sequence differentially regulate protein secretion from proteolysis, J. Biol. Chem, 289, 29030, 10.1074/jbc.M114.594861 · DOI
  15. Hall, 2012, Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate, ACS Chem. Biol, 7, 1848, 10.1021/cb3002478 · DOI
  16. Benjannet, 2006, The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications, J. Biol. Chem, 281, 30561, 10.1074/jbc.M606495200 · DOI · Paper page
  17. Zhao, 2006, Molecular characterization of loss-of-function mutations in PCSK9 and identification of a compound heterozygote, Am. J. Hum. Genet, 79, 514, 10.1086/507488 · DOI
  18. Kim, 2011, High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice, PLoS One, 6, e18556, 10.1371/journal.pone.0018556 · DOI
  19. Hasson, 2015, Chemogenomic profiling of endogenous PARK2 expression using a genome-edited coincidence reporter, ACS Chem. Biol, 10, 1188, 10.1021/cb5010417 · DOI
  20. Benjannet, 2004, NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol, J. Biol. Chem, 279, 48865, 10.1074/jbc.M409699200 · DOI · Paper page
  21. Engler, 2008, A one pot, one step, precision cloning method with high throughput capability, PLoS One, 3, e3647, 10.1371/journal.pone.0003647 · DOI
  22. Cong, 2015, Genome engineering using CRISPR-Cas9 system, Methods Mol. Biol, 1239, 197, 10.1007/978-1-4939-1862-1_10 · DOI
  23. Benjannet, 2012, Loss- and gain-of-function Pcsk9 variants: cleavage specificity, dominant negative effects, and low density lipoprotein receptor (LDLR) degradation, J. Biol. Chem, 287, 33745, 10.1074/jbc.M112.399725 · DOI
  24. Garvie, 2016, Point mutations at the catalytic site of PCSK9 inhibit folding, autoprocessing, and interaction with the LDL receptor, Protein Sci, 25, 2018, 10.1002/pro.3019 · DOI
  25. Crooks, 2004, WebLogo: a sequence logo generator, Genome Res, 14, 1188, 10.1101/gr.849004 · DOI
  26. Cameron, 2008, Investigations on the evolutionary conservation of PCSK9 reveal a functionally important protrusion, FEBS J, 275, 4121, 10.1111/j.1742-4658.2008.06553.x · DOI
  27. Zhang, 2017, Discovery of a cryptic peptide-binding site on PCSK9 and design of antagonists, Nat. Struct. Mol. Biol, 24, 848, 10.1038/nsmb.3453 · DOI
  28. McNutt, 2007, Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells, J. Biol. Chem, 282, 20799, 10.1074/jbc.C700095200 · DOI · Paper page
  29. Cameron, 2009, Mutation S462P in the PCSK9 gene reduces secretion of mutant PCSK9 without affecting the autocatalytic cleavage, Atherosclerosis, 203, 161, 10.1016/j.atherosclerosis.2008.10.007 · DOI
  30. Leigh, 2009, Commentary PCSK9 variants: a new database, Atherosclerosis, 203, 32, 10.1016/j.atherosclerosis.2009.02.006 · DOI
  31. Landrum, 2016, ClinVar: public archive of interpretations of clinically relevant variants, Nucleic Acids Res, 44, D862, 10.1093/nar/gkv1222 · DOI · Paper page
  32. Kwon, 2008, Molecular basis for LDL receptor recognition by PCSK9, Proc. Natl. Acad. Sci. U.S.A, 105, 1820, 10.1073/pnas.0712064105 · DOI · Paper page
  33. Cameron, 2006, Effect of mutations in the PCSK9 gene on the cell surface LDL receptors, Hum. Mol. Genet, 15, 1551, 10.1093/hmg/ddl077 · DOI · Paper page
  34. Cameron, 2008, Characterization of novel mutations in the catalytic domain of the PCSK9 gene, J. Intern. Med, 263, 420, 10.1111/j.1365-2796.2007.01915.x · DOI
  35. McNutt, 2009, Antagonism of secreted PCSK9 increases low density lipoprotein receptor expression in HepG2 cells, J. Biol. Chem, 284, 10561, 10.1074/jbc.M808802200 · DOI
  36. Homer, 2008, Identification and characterization of two non-secreted PCSK9 mutants associated with familial hypercholesterolemia in cohorts from New Zealand and South Africa, Atherosclerosis, 196, 659, 10.1016/j.atherosclerosis.2007.07.022 · DOI · Paper page
  37. Du, 2011, Novel domain interaction regulates secretion of proprotein convertase subtilisin/kexin type 9 (PCSK9) protein, J. Biol. Chem, 286, 43054, 10.1074/jbc.M111.273474 · DOI
  38. Niers, 2011, Multimodal in vivo imaging and blood monitoring of intrinsic and extrinsic apoptosis, Mol. Ther, 19, 1090, 10.1038/mt.2011.17 · DOI
  39. Ketteler, 2008, A pathway sensor for genome-wide screens of intracellular proteolytic cleavage, Genome Biol, 9, R64, 10.1186/gb-2008-9-4-r64 · DOI
  40. Qu, 2014, Development of a Gaussia luciferase-based human norovirus protease reporter system: cell type-specific profile of Norwalk virus protease precursors and evaluation of inhibitors, J. Virol, 88, 10312, 10.1128/JVI.01111-14 · DOI
  41. Bartok, 2013, iGLuc: a luciferase-based inflammasome and protease activity reporter, Nat. Methods, 10, 147, 10.1038/nmeth.2327 · DOI
  42. Miyake, 2008, Genetic variants in PCSK9 in the Japanese population: rare genetic variants in PCSK9 might collectively contribute to plasma LDL cholesterol levels in the general population, Atherosclerosis, 196, 29, 10.1016/j.atherosclerosis.2006.12.035 · DOI
  43. Lakoski, 2009, Genetic and metabolic determinants of plasma PCSK9 levels, J. Clin. Endocrinol. Metab, 94, 2537, 10.1210/jc.2009-0141 · DOI · Paper page
  44. Dubuc, 2010, A new method for measurement of total plasma PCSK9: clinical applications, J. Lipid Res, 51, 140, 10.1194/jlr.M900273-JLR200 · DOI
  45. Wanneh, 2017, Predicting proprotein convertase subtilisin kexin type-9 loss of function mutations using plasma PCSK9 concentration, J. Clin. Lipidol, 11, 55, 10.1016/j.jacl.2016.09.015 · DOI
  46. Persson, 2010, Circulating proprotein convertase subtilisin kexin type 9 has a diurnal rhythm synchronous with cholesterol synthesis and is reduced by fasting in humans, Arterioscler. Thromb. Vasc. Biol, 30, 2666, 10.1161/ATVBAHA.110.214130 · DOI · Paper page
  47. Cariou, 2013, Plasma PCSK9 concentrations during an oral fat load and after short term high-fat, high-fat high-protein and high-fructose diets, Nutr. Metab. (Lond.), 10, 4, 10.1186/1743-7075-10-4 · DOI
  48. Browning, 2010, Fasting reduces plasma proprotein convertase, subtilisin/kexin type 9 and cholesterol biosynthesis in humans, J. Lipid Res, 51, 3359, 10.1194/jlr.P009860 · DOI
  49. Lagace, 2006, Secreted PCSK9 decreases the number of LDL receptors in hepatocytes and in livers of parabiotic mice, J. Clin. Invest, 116, 2995, 10.1172/JCI29383 · DOI · Paper page
  50. Essalmani, 2011, In vivo evidence that furin from hepatocytes inactivates PCSK9, J. Biol. Chem, 286, 4257, 10.1074/jbc.M110.192104 · DOI · Paper page
  51. Ai, 2016, C-terminal loop mutations determine folding and secretion properties of PCSK9, Biochem. Mol. Biol. J, 2, 17, 10.21767/2471-8084.100026 · DOI
  52. Horton, 2003, Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes, Proc. Natl. Acad. Sci. U.S.A, 100, 12027, 10.1073/pnas.1534923100 · DOI · Paper page
  53. Dubuc, 2004, Statins upregulate PCSK9, the gene encoding the proprotein convertase neural apoptosis-regulated convertase-1 implicated in familial hypercholesterolemia, Arterioscler. Thromb. Vasc. Biol, 24, 1454, 10.1161/01.ATV.0000134621.14315.43 · DOI · Paper page
  54. Lochhead, 2005, Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs, Cell, 121, 925, 10.1016/j.cell.2005.03.034 · DOI
  55. Foote, 1985, Substrate specificity of aspartate transcarbamylase: interaction of the enzyme with analogs of aspartate and succinate, J. Biol. Chem, 260, 9624, 10.1016/S0021-9258(17)39283-9 · DOI
  56. Joshi, 2013, Kinetic and structural investigations into the allosteric and pH effect on the substrate specificity of human epithelial 15-lipoxygenase-2, Biochemistry, 52, 8026, 10.1021/bi4010649 · DOI
  57. Shelton, 2009, Modulation of γ-secretase specificity using small molecule allosteric inhibitors, Proc. Natl. Acad. Sci. U.S.A, 106, 20228, 10.1073/pnas.0910757106 · DOI
  58. Gibson, 2009, Enzymatic assembly of DNA molecules up to several hundred kilobases, Nat. Methods, 6, 343, 10.1038/nmeth.1318 · DOI
  59. Liu, 2008, An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol, BMC Biotechnol, 8, 91, 10.1186/1472-6750-8-91 · DOI
  60. Zhang, 1999, A simple statistical parameter for use in evaluation and validation of high throughput screening assays, J. Biomol. Screen, 4, 67, 10.1177/108705719900400206 · DOI · Paper page
  61. Fiser, 2003, ModLoop: automated modeling of loops in protein structures, Bioinformatics, 19, 2500, 10.1093/bioinformatics/btg362 · DOI

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Metadata

Authors
Chorba, J. S., Galvan, A. M., & Shokat, K. M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2018-02
Volume
293
Issue
6
Pages
1875-1886
ISSN
0021-9258
DOI
10.1074/jbc.ra117.000754
Cited by
18
References
2
Language
en
Update notices
correction (2018-05-04)
Licence
Funders
  • Howard Hughes Medical Institute (HHMI) (Medical Student Fellowship)
  • HHS NIH National Heart, Lung, and Blood Institute (NHLBI) (K08 HL124068 and LRP HMOT1243)
  • HHS NIH National Center for Advancing Translational Sciences (NCATS) (UL1 TR000004)
  • Academic Senate, University of California, San Francisco
  • Hellman Foundation
  • Gilead Sciences (Gilead) (Research Scholar in Cardiovascular Diseases)
  • Pfizer Inc. Pfizer Foundation (ASPIRE Cardiovascular Award)
  • Clinical and Translational Science Institute, University of California, San Francisco (CTSI) (UL1 TR000004)

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