Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén
Transient receptor potential mucolipin (TRPML) protein in flies plays a pivotal role in Ca<sup>2+</sup> ions release, resulting in membrane trafficking, autophagy and ion homeostasis. However, to date, the characterization of TRPML in agricultural pests remains unknown. Here, we firstly...
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2021-12-01
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author | Haitao Wang Yan Dong Baijie Wan Yinghua Ji Qiufang Xu |
author_facet | Haitao Wang Yan Dong Baijie Wan Yinghua Ji Qiufang Xu |
author_sort | Haitao Wang |
collection | DOAJ |
description | Transient receptor potential mucolipin (TRPML) protein in flies plays a pivotal role in Ca<sup>2+</sup> ions release, resulting in membrane trafficking, autophagy and ion homeostasis. However, to date, the characterization of TRPML in agricultural pests remains unknown. Here, we firstly reported the TRPML of a destructive pest of gramineous crops, <i>Laodelphax striatellus</i>. The <i>L</i>. <i>striatellus</i> TRPML (Ls-TRPML) has a 1818 bp open reading frame, encoding 605 amino acid. TRPML in agricultural pests is evolutionarily conserved, and the expression of Ls-TRPML is predominately higher in the ovary than in other organs of <i>L</i>. <i>striatellus</i> at the transcript and protein level. The Bac–Bac system showed that Ls-TRPML localized in the plasma membrane, nuclear membrane and nucleus and co-localized with lysosome in <i>Spodoptera frugiperda</i> cells. The immunofluorescence microscopy analysis showed that Ls-TRPML localized in the cytoplasm and around the nuclei of the intestine cells or ovary follicular cells of <i>L</i>. <i>striatellus</i>. The results from the lipid-binding assay revealed that Ls-TRPML strongly bound to phosphatidylinositol-3,5-bisphosphate, as compared with other phosphoinositides. Overall, our results helped is identify and characterize the TRPML protein of <i>L</i>. <i>striatellus</i>, shedding light on the function of TRPML in multiple cellular processes in agricultural pests. |
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spelling | doaj.art-e66fa928bc5049aca658754088095dd92023-11-23T08:52:58ZengMDPI AGInsects2075-44502021-12-011212110710.3390/insects12121107Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> FallénHaitao Wang0Yan Dong1Baijie Wan2Yinghua Ji3Qiufang Xu4Key Laboratory of Food Quality and Safety of Jiangsu Province, Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaKey Laboratory of Food Quality and Safety of Jiangsu Province, Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaInstitute of Agricultural Sciences in Jiangsu Coastal Area, Yancheng 224002, ChinaKey Laboratory of Food Quality and Safety of Jiangsu Province, Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaKey Laboratory of Food Quality and Safety of Jiangsu Province, Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaTransient receptor potential mucolipin (TRPML) protein in flies plays a pivotal role in Ca<sup>2+</sup> ions release, resulting in membrane trafficking, autophagy and ion homeostasis. However, to date, the characterization of TRPML in agricultural pests remains unknown. Here, we firstly reported the TRPML of a destructive pest of gramineous crops, <i>Laodelphax striatellus</i>. The <i>L</i>. <i>striatellus</i> TRPML (Ls-TRPML) has a 1818 bp open reading frame, encoding 605 amino acid. TRPML in agricultural pests is evolutionarily conserved, and the expression of Ls-TRPML is predominately higher in the ovary than in other organs of <i>L</i>. <i>striatellus</i> at the transcript and protein level. The Bac–Bac system showed that Ls-TRPML localized in the plasma membrane, nuclear membrane and nucleus and co-localized with lysosome in <i>Spodoptera frugiperda</i> cells. The immunofluorescence microscopy analysis showed that Ls-TRPML localized in the cytoplasm and around the nuclei of the intestine cells or ovary follicular cells of <i>L</i>. <i>striatellus</i>. The results from the lipid-binding assay revealed that Ls-TRPML strongly bound to phosphatidylinositol-3,5-bisphosphate, as compared with other phosphoinositides. Overall, our results helped is identify and characterize the TRPML protein of <i>L</i>. <i>striatellus</i>, shedding light on the function of TRPML in multiple cellular processes in agricultural pests.https://www.mdpi.com/2075-4450/12/12/1107<i>Laodelphax striatellus</i>TRPMLexpression profilesubcellular localizationlipid binding |
spellingShingle | Haitao Wang Yan Dong Baijie Wan Yinghua Ji Qiufang Xu Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén Insects <i>Laodelphax striatellus</i> TRPML expression profile subcellular localization lipid binding |
title | Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén |
title_full | Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén |
title_fullStr | Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén |
title_full_unstemmed | Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén |
title_short | Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of <i>Laodelphax striatellus</i> Fallén |
title_sort | identification and characterization analysis of transient receptor potential mucolipin protein of i laodelphax striatellus i fallen |
topic | <i>Laodelphax striatellus</i> TRPML expression profile subcellular localization lipid binding |
url | https://www.mdpi.com/2075-4450/12/12/1107 |
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