New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET
Human CISD2 and mitoNEET are two NEET proteins anchored in the endoplasmic reticulum and mitochondria membranes respectively, with an Fe–S containing domain stretching out in the cytosol. Their cytosolic domains are close in sequence and structure. In the present study, combining cellular and bioche...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-04-01
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| Series: | Biomedicines |
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| Online Access: | https://www.mdpi.com/2227-9059/9/4/384 |
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| author | Myriam Salameh Sylvie Riquier Olivier Guittet Meng-Er Huang Laurence Vernis Michel Lepoivre Marie-Pierre Golinelli-Cohen |
| author_facet | Myriam Salameh Sylvie Riquier Olivier Guittet Meng-Er Huang Laurence Vernis Michel Lepoivre Marie-Pierre Golinelli-Cohen |
| author_sort | Myriam Salameh |
| collection | DOAJ |
| description | Human CISD2 and mitoNEET are two NEET proteins anchored in the endoplasmic reticulum and mitochondria membranes respectively, with an Fe–S containing domain stretching out in the cytosol. Their cytosolic domains are close in sequence and structure. In the present study, combining cellular and biochemical approaches, we compared both proteins in order to possibly identify specific roles and mechanisms of action in the cell. We show that both proteins exhibit a high intrinsic stability and a sensitivity of their cluster to oxygen. In contrast, they differ in according to expression profiles in tissues and intracellular half-life. The stability of their Fe–S cluster and its ability to be transferred in vitro are affected differently by pH variations in a physiological and pathological range for cytosolic pH. Finally, we question a possible role for CISD2 in cellular Fe–S cluster trafficking. In conclusion, our work highlights unexpected major differences in the cellular and biochemical features between these two structurally close NEET proteins. |
| first_indexed | 2024-03-10T12:36:08Z |
| format | Article |
| id | doaj.art-c9d899e8270e40c0884d6193ae1f9bd9 |
| institution | Directory Open Access Journal |
| issn | 2227-9059 |
| language | English |
| last_indexed | 2024-03-10T12:36:08Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomedicines |
| spelling | doaj.art-c9d899e8270e40c0884d6193ae1f9bd92023-11-21T14:16:50ZengMDPI AGBiomedicines2227-90592021-04-019438410.3390/biomedicines9040384New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEETMyriam Salameh0Sylvie Riquier1Olivier Guittet2Meng-Er Huang3Laurence Vernis4Michel Lepoivre5Marie-Pierre Golinelli-Cohen6CNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceCNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceCNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceCNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceCNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceCNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceCNRS, Institut de Chimie des Substances Naturelles, Université Paris-Saclay, UPR 2301, 91198 Gif-sur-Yvette, FranceHuman CISD2 and mitoNEET are two NEET proteins anchored in the endoplasmic reticulum and mitochondria membranes respectively, with an Fe–S containing domain stretching out in the cytosol. Their cytosolic domains are close in sequence and structure. In the present study, combining cellular and biochemical approaches, we compared both proteins in order to possibly identify specific roles and mechanisms of action in the cell. We show that both proteins exhibit a high intrinsic stability and a sensitivity of their cluster to oxygen. In contrast, they differ in according to expression profiles in tissues and intracellular half-life. The stability of their Fe–S cluster and its ability to be transferred in vitro are affected differently by pH variations in a physiological and pathological range for cytosolic pH. Finally, we question a possible role for CISD2 in cellular Fe–S cluster trafficking. In conclusion, our work highlights unexpected major differences in the cellular and biochemical features between these two structurally close NEET proteins.https://www.mdpi.com/2227-9059/9/4/384iron-sulfur proteinCISD2Fe–S cluster transferFe–S cluster labilityWolfram syndromeUV-visible absorption spectroscopy |
| spellingShingle | Myriam Salameh Sylvie Riquier Olivier Guittet Meng-Er Huang Laurence Vernis Michel Lepoivre Marie-Pierre Golinelli-Cohen New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET Biomedicines iron-sulfur protein CISD2 Fe–S cluster transfer Fe–S cluster lability Wolfram syndrome UV-visible absorption spectroscopy |
| title | New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET |
| title_full | New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET |
| title_fullStr | New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET |
| title_full_unstemmed | New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET |
| title_short | New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET |
| title_sort | new insights of the neet protein cisd2 reveals distinct features compared to its close mitochondrial homolog mitoneet |
| topic | iron-sulfur protein CISD2 Fe–S cluster transfer Fe–S cluster lability Wolfram syndrome UV-visible absorption spectroscopy |
| url | https://www.mdpi.com/2227-9059/9/4/384 |
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