Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition
Abstract
:1. Overview of Centrins
2. Centrins Have Large Differences in Their Ability to Sense Ca2+
Organism | Centrin | UniProt Code | Experimental Ca2+-Binding Sites a | Ca2+ Affinity b | Refs |
---|---|---|---|---|---|
Chlamydomonas reinhardtii | CrCEN | P05434 | 4 | Kd1,2N = 1.2 ± 0.1 × 10−6 M Kd3C = 2 ± 2 × 10−5 M Kd4C = 3 ± 2 × 10−3 M | [64,65,66] |
Scherffelia dubia | SdCEN | Q06827 | 3 | Ka1N = 2.6 × 105 M−1 Ka2N = 4.3 × 105 M−1 Ka3C = 1.1 × 105 M−1 | [52] |
Homo sapiens | HsCEN1 | Q12798 | 4 | Ka1,2 = 4.26 × 105 ± 9.5 × 104 M−1 Ka3,4 = 2.73 × 104 ± 2.7 × 103 M−1 | [67,68] |
Homo sapiens | HsCEN2 | P41208 | 2 | Ka(EF-3) = 8.1 × 103 M−1 Ka(EF-4) = 1.5 × 105 M−1 | [43,48,49,50,62] |
Homo sapiens | HsCEN3 | O15182 | 3 | Ka1N = 3.3 × 105 M−1 Ka2 = 7.0 × 103 M−1 Ka3 = 7.5 × 103 M−1 | [69] |
Saccharomyces cerevisiae | CDC31 | P06704 | 3 | Ka(EF-1) = 3.0 × 106 M−1 Ka2C = 2.4 × 104 M−1 Ka3C = 3.5 × 104 M−1 | [19,70] |
Mus musculus | MmCEN1 | P41209 | 4 | Ka1 = 5.23 × 105 M−1 Ka2 = 3.11 × 103 M−1 Ka3 = 2.31 × 105 M−1 Ka4 = 1.59 × 104 M−1 | [51] |
Arabidopsis thaliana | AtCEN2 | O23184 | 4 | Ka(EF-1) = 2.9 × 105 ± 7.1 × 104 M−1 Ka(EF-2) = 4.1 × 105 ± 6.8 × 104 M−1 Ka(EF-3) = 1.4 × 104 ± 3.8 × 103 M−1 Ka(EF-4) = 3.7 × 103 ± 0.8 × 103 M−1 | [22] |
Toxoplasma gondii | TgCEN1 | A0A125YHX7 | 2 | Ka(EF-1) = 4.8 × 105 ± 6.1 × 103 M−1 Ka(EF-2) = 3.9 × 104 ± 4.5 × 103 M−1 | [53] |
Toxoplasma gondii | TgCEN2 | A0A125YZN2 | 1 | Ka(EF-1) = 1.6 × 104 ± 1.5 × 103 M−1 | [53] |
Trypanosoma brucei | TbCEN4 | A0A3L6L623 | 2 | Ka(EF-3) = 3.18 × 105 ± 4.63 × 104 M−1 Ka(EF-4) = 2.63 × 104 ± 4.37 × 103 M−1 | [14] |
Trypanosoma brucei | TbCEN5 | Q382E7 | 2 | Kd1,2 = 4.8 µM | [71] |
Euplotes octocarinatus | EoCEN | Q9XZV2 | 4 | Ka1,2 = 1.12 ± 0.04 × 103 M−1 Ka(EF-4) = 6.82 ± 0.33 × 105 M−1 | [13,72] |
Blastocladiella emersonii | BeCEN1 | Q4F6W6 | 4 | Kd1 = 6.06 ± 2.26 µM Kd2 = 7.50 ± 0.44 µM Kd3 = 75.20 ± 28.3 µM Kd4 = 9.35 ± 0.93 µM | [73] |
Blastocladiella emersonii | BeCEN3 | Q4F6W5 | 4 | Kd1 = 2.45 ± 0.04 µM Kd2 = 18.50 ± 0.86 µM Kd3 = 2.11 ± 0.38 µM Kd4 = 38.1 ± 7.46 µM | [73] |
3. Functional Diversity and Specialization of Centrins
Centrin | Identified Target | Complex Localization | Function/Pathway | Centrin Binding Motif of Targets | Target Binding Affinity a | PDB CODE | Refs |
---|---|---|---|---|---|---|---|
HsCEN2 | XPC | Nucleus | NER | 847-NWKLLAKGLLIRERLKR-863 | with Ca2+, Ka = 170 ± 30 × 106 M−1 without Ca2+, Ka = 8 ± 1 × 106 M−1 | 2GGM, 2OBH, 2A4J | [17,43,49,76,77,87] |
HsCEN2 | XPA | Nucleus | NER | N/A b | N/A | N/A | [87,88] |
CDC31 | RAD4 | Nucleus | DNA repair and protein degradation | N/A | N/A | N/A | [28] |
AtCEN2 | AtRAD4 | Nucleus | NER | 756-EAQAASRWYQLLSSILTR-773 | with Ca2+, Kd = 54 ± 14 nM without Ca2+, Kd = 8 ± 1 µM | N/A | [18,22] |
HsCEN1 | HsSFI1 (R18) c | Basal body/ centrosome | Centrosome duplication | 670-REVAARESQHNRQLLRGALRRWK-692 | with Ca2+, Ka = 12.03 × 105 M−1 without Ca2+, Ka = 0.03 × 105 M−1 | N/A | [29,89] |
HsCEN2 | HsSFI1(R17) | Basal body/ centrosome | Centrosome duplication | 641-RADLHHQHSVLHRALQAWVT-660 | with Ca2+, Ka = 6.5 ± 0.9 × 106 M−1 without Ca2+, Ka = 0.25 ± 0.02 × 106 M−1 | 2K2I | [29,78,90] |
CDC31 | ScSFI1 (R18) | SPB | SPB duplication | 680- IQAISKRNYQLEKMVLKKFR -699 | with Ca2+, Ka = 1 ± 0.03 × 107 M−1 without Ca2+, Ka = 2.4 ± 0.13 × 105 M−1 | 2GV5, 2DOQ | [19,70,74,91] |
CDC31 | ScSFI1 (R19) | SPB | SPB duplication | 710- ELADEVREEFVLVKTFYIWK -729 | with Ca2+, Ka = 3.5 ± 0.29 × 107 M−1 without Ca2+, Ka = 1.9 ± 0.3 × 105 M−1 | N/A | [19,70,74,91] |
HsCEN2 HsCEN3 | GANP | Nuclear pore | mRNA export | 1225-IFQTAKETLQELQCFCKYLQRWR-1247 | N/A | N/A | [20,25,92] |
CDC31 | SAC3 | Nuclear pore | mRNA export | 797-KFFEKWQASYSQAKKNRI-814 | with Ca2+, Ka = 2.2 ± 0.2 × 107 M−1 without Ca2+, Ka = 1.5 ± 0.11 × 106 M−1 | 3FWB, 3FWC, 4MBE | [19,20,24,93,94] |
AtCEN1 AtCEN2 | SAC3B | Nuclear pore | mRNA export | 1050-AKAKLKLIIRLWKRWSSRQSELRERR-1075 | with Ca2+, Ka = 1.5 x 106 ± 5.5 × 105 M−1 without Ca2+, Ka = 4.1 x 105 ± 8.3 × 104 M−1 | N/A | [21,95,96] |
CDC31 | KAR1 | SPB | SPB duplication | 237-KKRELIESKWHRLLFHDKK-255 | with Ca2+, Ka = 2.3 ± 0.15 × 107 M−1 without Ca2+, Ka = 4.4 ± 0.1 × 105 M−1 | N/A | [8,19,80,97] |
HsCEN1 | Transducin β | Photoreceptor Connecting Cilium | Phototransduction | 325-MAVATGSWDSFLKIWN-340 | with Ca2+, Ka = 0.17 ± 0.12 × 106 M−1 | N/A | [23,29,84] |
HsCEN2 | POC5 | Basal body/ centrosome | Centriole elongation | 156-LQKMENVLDLWSSGLKTN-173 245-KIELMRTFFHWRIGHVRA-262 278-RTLLKKVWKVWRSVVQKQ-295 | N/A | N/A | [98,99] |
HsCEN2 | PRP40A | Nucleus | Pre-mRNA splicing | 524-KQLRKRNWEALKNILDNMANVTYSTTWSEAQQY-556 | with Ca2+, Ka = 3.6 x ± 0.4 × 106 M−1 | N/A | [75] |
HsCEN2 | NUP107-160 | Nuclear pore | mRNA and protein nuclear export | N/A | N/A | N/A | [25] |
HsCEN2 | MPS1 | Centrosome | Centriole assembly | N/A | N/A | N/A | [100] |
HsCEN3 | MPS1 | Centrosome | Inhibition of centrosome duplication | N/A | N/A | N/A | [101] |
CDC31 | MPS3p | SPB | SPB duplication | N/A | N/A | N/A | [102] |
HsCEN2 | CP110 | Centrosome | Cytokinesis | N/A | N/A | N/A | [103] |
HsCEN2 | CDC25B | Centrosome Cytoplasm | Centrosome integrity | N/A | N/A | N/A | [104,105] |
HsCEN2 | Gelectin-3 | Centrosome | N/A | N/A | N/A | N/A | [106] |
CDC31 | KIC1p | N/A | Cell integrity/ morphogenesis | N/A | N/A | N/A | [107,108] |
CDC31 | 26S proteasome | Cytoplasm/ proteasome | Protein degradation | N/A | N/A | N/A | [28] |
CDC31 | cytosolic and mitochondrial factors | Mitochondria | Energy metabolism | N/A | N/A | N/A | [109] |
CDC31 | VPS13 | N/A | TGN (trans-Golgi network) –PVC (prevacuolar compartment) transport and TGN homotypic fusion | N/A | N/A | N/A | [110,111] |
AtCEN1 | Tonneau1 | Cytoskeleton | microtubule centers organization | N/A | N/A | N/A | [1] |
4. Centrin–Peptide Complexes
4.1. Centrins and Nucleotide Excision Repair
4.2. SFI1 and Centrosome Duplication
4.3. Centrins and mRNA Export
4.4. Centrins and KAR1
5. Conclusions and Future Directions
Author Contributions
Funding
Conflicts of Interest
References
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Pedretti, M.; Bombardi, L.; Conter, C.; Favretto, F.; Dominici, P.; Astegno, A. Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition. Int. J. Mol. Sci. 2021, 22, 12173. https://doi.org/10.3390/ijms222212173
Pedretti M, Bombardi L, Conter C, Favretto F, Dominici P, Astegno A. Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition. International Journal of Molecular Sciences. 2021; 22(22):12173. https://doi.org/10.3390/ijms222212173
Chicago/Turabian StylePedretti, Marco, Luca Bombardi, Carolina Conter, Filippo Favretto, Paola Dominici, and Alessandra Astegno. 2021. "Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition" International Journal of Molecular Sciences 22, no. 22: 12173. https://doi.org/10.3390/ijms222212173