Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
The double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) – the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) – a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2019-01-01
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| Series: | Nucleus |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/19491034.2019.1618175 |
| _version_ | 1818364054535667712 |
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| author | Li-Chun Cheng Sabyasachi Baboo Cory Lindsay Liza Brusman Salvador Martinez-Bartolomé Olga Tapia Xi Zhang John R. Yates Larry Gerace |
| author_facet | Li-Chun Cheng Sabyasachi Baboo Cory Lindsay Liza Brusman Salvador Martinez-Bartolomé Olga Tapia Xi Zhang John R. Yates Larry Gerace |
| author_sort | Li-Chun Cheng |
| collection | DOAJ |
| description | The double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) – the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) – a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in mesenchyme-derived cells, we used proteomics to characterize NE and other subcellular fractions isolated from mesenchymal stem cells and from adipocytes and myocytes. Based on spectral abundance, we calculated enrichment scores for proteins in the NE fractions. We demonstrated by quantitative immunofluorescence microscopy that five little-characterized proteins with high enrichment scores are substantially concentrated at the NE, with Itprip exposed at the outer nuclear membrane, Smpd4 enriched at the NPC, and Mfsd10, Tmx4, and Arl6ip6 likely residing in the inner nuclear membrane. These proteins provide new focal points for studying the functions of the NE. Moreover, our datasets provide a resource for evaluating additional potential NE proteins. |
| first_indexed | 2024-12-13T21:58:16Z |
| format | Article |
| id | doaj.art-09ae6449b3284cc385b3e7503139eb59 |
| institution | Directory Open Access Journal |
| issn | 1949-1034 1949-1042 |
| language | English |
| last_indexed | 2024-12-13T21:58:16Z |
| publishDate | 2019-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Nucleus |
| spelling | doaj.art-09ae6449b3284cc385b3e7503139eb592022-12-21T23:30:05ZengTaylor & Francis GroupNucleus1949-10341949-10422019-01-0110112614310.1080/19491034.2019.16181751618175Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cellsLi-Chun Cheng0Sabyasachi Baboo1Cory Lindsay2Liza Brusman3Salvador Martinez-Bartolomé4Olga Tapia5Xi Zhang6John R. Yates7Larry Gerace8The Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe Scripps Research InstituteThe double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) – the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) – a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in mesenchyme-derived cells, we used proteomics to characterize NE and other subcellular fractions isolated from mesenchymal stem cells and from adipocytes and myocytes. Based on spectral abundance, we calculated enrichment scores for proteins in the NE fractions. We demonstrated by quantitative immunofluorescence microscopy that five little-characterized proteins with high enrichment scores are substantially concentrated at the NE, with Itprip exposed at the outer nuclear membrane, Smpd4 enriched at the NPC, and Mfsd10, Tmx4, and Arl6ip6 likely residing in the inner nuclear membrane. These proteins provide new focal points for studying the functions of the NE. Moreover, our datasets provide a resource for evaluating additional potential NE proteins.http://dx.doi.org/10.1080/19491034.2019.1618175nuclear envelopenuclear pore complex (npc)proteomicsmesenchymal stem cell (msc)adipocytemyocyte |
| spellingShingle | Li-Chun Cheng Sabyasachi Baboo Cory Lindsay Liza Brusman Salvador Martinez-Bartolomé Olga Tapia Xi Zhang John R. Yates Larry Gerace Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells Nucleus nuclear envelope nuclear pore complex (npc) proteomics mesenchymal stem cell (msc) adipocyte myocyte |
| title | Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells |
| title_full | Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells |
| title_fullStr | Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells |
| title_full_unstemmed | Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells |
| title_short | Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells |
| title_sort | identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells |
| topic | nuclear envelope nuclear pore complex (npc) proteomics mesenchymal stem cell (msc) adipocyte myocyte |
| url | http://dx.doi.org/10.1080/19491034.2019.1618175 |
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