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Monomer/dimer transition of the caspase-recruitment domain of human Nod1.

Srimathi T, Robbins SL, Dubas RL, Hasegawa M, Inohara N, Park YC
Biochemistry 47 1319-25 (2008)
Cited: 39 times
EuropePMC logo PMID: 18186648

Abstract

Nod1 is an essential cytoplasmic sensor for bacterial peptidoglycans in the innate immune system. The caspase-recruitment domain of Nod1 (Nod1_CARD) is indispensable for recruiting a downstream kinase, receptor-interacting protein 2 (RIP2), that activates nuclear factor-kappaB (NF-kappaB). The crystal structure of human Nod1_CARD at 1.9 A resolution reveals a novel homodimeric conformation. Our structural and biochemical analysis shows that the homodimerization of Nod1_CARD is achieved by swapping the H6 helices at the carboxy termini and stabilized by forming an interchain disulfide bond between the Cys39 residues of the two monomers in solution and in the crystal. In addition, we present experimental evidence for a pH-sensitive conformational change of Nod1_CARD. Our results suggest that the pH-sensitive monomer/dimer transition is a unique molecular property of Nod1_CARD.

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  1. Structural mechanisms in NLR inflammasome signaling. Lechtenberg BC, Mace PD, Riedl SJ. Curr Opin Struct Biol 29 17-25 (2014)
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  8. The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces. Jin T, Huang M, Smith P, Jiang J, Xiao TS. Acta Crystallogr Sect F Struct Biol Cryst Commun 69 482-487 (2013)
  9. The enigma of the near-symmetry of proteins: Domain swapping. Bonjack-Shterengartz M, Avnir D. PLoS One 12 e0180030 (2017)
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Reviews citing this publication (5)

  1. NLR functions in plant and animal immune systems: so far and yet so close. Maekawa T, Kufer TA, Schulze-Lefert P. Nat Immunol 12 817-826 (2011)
  2. Insights into the molecular basis of the NOD2 signalling pathway. Boyle JP, Parkhouse R, Monie TP. Open Biol 4 140178 (2014)
  3. The versatile roles of CARDs in regulating apoptosis, inflammation, and NF-κB signaling. Kao WP, Yang CY, Su TW, Wang YT, Lo YC, Lin SC. Apoptosis 20 174-195 (2015)
  4. Structure and regulation of cytoplasmic adapter proteins involved in innate immune signaling. Monie TP, Moncrieffe MC, Gay NJ. Immunol Rev 227 161-175 (2009)
  5. Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF). Park YH, Jeong MS, Jang SB. BMB Rep 49 159-166 (2016)

Articles citing this publication (16)

  1. Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly. Bae JY, Park HH. J Biol Chem 286 39528-39536 (2011)
  2. CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses cell proliferation and migration. Lopez J, John SW, Tenev T, Rautureau GJ, Hinds MG, Francalanci F, Wilson R, Broemer M, Santoro MM, Day CL, Meier P. Mol Cell 42 569-583 (2011)
  3. L-Ala-γ-D-Glu-meso-diaminopimelic acid (DAP) interacts directly with leucine-rich region domain of nucleotide-binding oligomerization domain 1, increasing phosphorylation activity of receptor-interacting serine/threonine-protein kinase 2 and its interaction with nucleotide-binding oligomerization domain 1. Laroui H, Yan Y, Narui Y, Ingersoll SA, Ayyadurai S, Charania MA, Zhou F, Wang B, Salaita K, Sitaraman SV, Merlin D. J Biol Chem 286 31003-31013 (2011)
  4. Daedalus: a robust, turnkey platform for rapid production of decigram quantities of active recombinant proteins in human cell lines using novel lentiviral vectors. Bandaranayake AD, Correnti C, Ryu BY, Brault M, Strong RK, Rawlings DJ. Nucleic Acids Res 39 e143 (2011)
  5. Evaluation of Nod-like receptor (NLR) effector domain interactions. Wagner RN, Proell M, Kufer TA, Schwarzenbacher R. PLoS One 4 e4931 (2009)
  6. Mutational analysis of human NOD1 and NOD2 NACHT domains reveals different modes of activation. Zurek B, Proell M, Wagner RN, Schwarzenbacher R, Kufer TA. Innate Immun 18 100-111 (2012)
  7. Interaction patches of procaspase-1 caspase recruitment domains (CARDs) are differently involved in procaspase-1 activation and receptor-interacting protein 2 (RIP2)-dependent nuclear factor κB signaling. Kersse K, Lamkanfi M, Bertrand MJM, Vanden Berghe T, Vandenabeele P. J Biol Chem 286 35874-35882 (2011)
  8. Structural and functional analysis of the NLRP4 pyrin domain. Eibl C, Grigoriu S, Hessenberger M, Wenger J, Puehringer S, Pinheiro AS, Wagner RN, Proell M, Reed JC, Page R, Diederichs K, Peti W. Biochemistry 51 7330-7341 (2012)
  9. Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2. Ver Heul AM, Fowler CA, Ramaswamy S, Piper RC. J Biol Chem 288 6890-6902 (2013)
  10. Cooperative regulation of NOTCH1 protein-phosphatidylinositol 3-kinase (PI3K) signaling by NOD1, NOD2, and TLR2 receptors renders enhanced refractoriness to transforming growth factor-beta (TGF-beta)- or cytotoxic T-lymphocyte antigen 4 (CTLA-4)-mediated impairment of human dendritic cell maturation. Ghorpade DS, Kaveri SV, Bayry J, Balaji KN. J Biol Chem 286 31347-31360 (2011)
  11. Crystal structure of myeloid cell activating receptor leukocyte Ig-like receptor A2 (LILRA2/ILT1/LIR-7) domain swapped dimer: molecular basis for its non-binding to MHC complexes. Chen Y, Gao F, Chu F, Peng H, Zong L, Liu Y, Tien P, Gao GF. J Mol Biol 386 841-853 (2009)
  12. Oligomeric structure of the MALT1 tandem Ig-like domains. Qiu L, Dhe-Paganon S. PLoS One 6 e23220 (2011)
  13. Novel disulfide bond-mediated dimerization of the CARD domain was revealed by the crystal structure of CARMA1 CARD. Jang TH, Park JH, Park HH. PLoS One 8 e79778 (2013)
  14. Structural basis for dimerization of the death effector domain of the F122A mutant of Caspase-8. Shen C, Pei J, Guo X, Zhou L, Li Q, Quan J. Sci Rep 8 16723 (2018)
  15. Coenzyme Q10 rescues ethanol-induced corneal fibroblast apoptosis through the inhibition of caspase-2 activation. Chen CC, Liou SW, Chen CC, Chen WC, Hu FR, Wang IJ, Lin SJ. J Biol Chem 288 11689-11704 (2013)
  16. The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized. Chen KE, Richards AA, Caradoc-Davies TT, Vajjhala PR, Robin G, Lua LH, Hill JM, Schroder K, Sweet MJ, Kellie S, Kobe B, Martin J. Acta Crystallogr D Biol Crystallogr 69 774-784 (2013)


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