Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins
Structure of interphase cell nuclei remains dynamic and can undergo various changes of shape and organisation, in health and disease. The double-membraned envelope that separates nuclear genetic material from the rest of the cell frequently includes deep, branching tubular invaginations that form a...
| Main Authors: | , , , , |
|---|---|
| Format: | Journal article |
| Published: |
Nature Publishing Group
2017
|
| _version_ | 1826299124821000192 |
|---|---|
| author | Drozdz, M Jiang, H Pytowski, L Grovenor, C Vaux, D |
| author_facet | Drozdz, M Jiang, H Pytowski, L Grovenor, C Vaux, D |
| author_sort | Drozdz, M |
| collection | OXFORD |
| description | Structure of interphase cell nuclei remains dynamic and can undergo various changes of shape and organisation, in health and disease. The double-membraned envelope that separates nuclear genetic material from the rest of the cell frequently includes deep, branching tubular invaginations that form a dynamic nucleoplasmic reticulum (NR). This study addresses mechanisms by which NR can form in interphase nuclei. We present a combination of Nanoscale Secondary Ion Mass Spectrometry (NanoSIMS) approach and light microscopy techniques to follow formation of NR by using pulse-chase experiments to examine protein and lipid delivery to nascent NR in cultured cells. Lamina protein incorporation was assessed using precursor accumulation (for lamin A) or a MAPLE3 photoconvertible tag (for lamin B1) and membrane phospholipid incorporation using stable isotope labelling with deuterated precursors followed by high resolution NanoSIMS. In all three cases, nascent molecules were selectively incorporated into newly forming NR tubules; thus strongly suggesting that NR formation is a regulated process involving a focal assembly machine, rather than simple physical perturbation of a pre-existing nuclear envelope. |
| first_indexed | 2024-03-07T04:57:09Z |
| format | Journal article |
| id | oxford-uuid:d6feedb7-118f-4385-a12c-10841741181e |
| institution | University of Oxford |
| last_indexed | 2024-03-07T04:57:09Z |
| publishDate | 2017 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | oxford-uuid:d6feedb7-118f-4385-a12c-10841741181e2022-03-27T08:37:44ZFormation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent laminsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d6feedb7-118f-4385-a12c-10841741181eSymplectic Elements at OxfordNature Publishing Group2017Drozdz, MJiang, HPytowski, LGrovenor, CVaux, DStructure of interphase cell nuclei remains dynamic and can undergo various changes of shape and organisation, in health and disease. The double-membraned envelope that separates nuclear genetic material from the rest of the cell frequently includes deep, branching tubular invaginations that form a dynamic nucleoplasmic reticulum (NR). This study addresses mechanisms by which NR can form in interphase nuclei. We present a combination of Nanoscale Secondary Ion Mass Spectrometry (NanoSIMS) approach and light microscopy techniques to follow formation of NR by using pulse-chase experiments to examine protein and lipid delivery to nascent NR in cultured cells. Lamina protein incorporation was assessed using precursor accumulation (for lamin A) or a MAPLE3 photoconvertible tag (for lamin B1) and membrane phospholipid incorporation using stable isotope labelling with deuterated precursors followed by high resolution NanoSIMS. In all three cases, nascent molecules were selectively incorporated into newly forming NR tubules; thus strongly suggesting that NR formation is a regulated process involving a focal assembly machine, rather than simple physical perturbation of a pre-existing nuclear envelope. |
| spellingShingle | Drozdz, M Jiang, H Pytowski, L Grovenor, C Vaux, D Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| title | Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| title_full | Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| title_fullStr | Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| title_full_unstemmed | Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| title_short | Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| title_sort | formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins |
| work_keys_str_mv | AT drozdzm formationofanucleoplasmicreticulumrequiresdenovoassemblyofnascentphospholipidsandshowspreferentialincorporationofnascentlamins AT jiangh formationofanucleoplasmicreticulumrequiresdenovoassemblyofnascentphospholipidsandshowspreferentialincorporationofnascentlamins AT pytowskil formationofanucleoplasmicreticulumrequiresdenovoassemblyofnascentphospholipidsandshowspreferentialincorporationofnascentlamins AT grovenorc formationofanucleoplasmicreticulumrequiresdenovoassemblyofnascentphospholipidsandshowspreferentialincorporationofnascentlamins AT vauxd formationofanucleoplasmicreticulumrequiresdenovoassemblyofnascentphospholipidsandshowspreferentialincorporationofnascentlamins |