Journal
JOURNAL OF CELL SCIENCE
Volume 124, Issue 24, Pages 4253-4266Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.091009
Keywords
Electron tomography; Nuclear lamina; Nucleoplasmic reticulum
Categories
Funding
- Medical Research Council [G0801917]
- MRC [G0801917] Funding Source: UKRI
- Medical Research Council [G0801917] Funding Source: researchfish
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Farnesylated prelamin A accumulates when the final endoproteolytic maturation of the protein fails to occur and causes a dysmorphic nuclear phenotype; however, the morphology and mechanisms of biogenesis of these changes remain unclear. We show here that acute prelamin A accumulation after reduction in the activity of the ZMPSTE24 endoprotease by short interfering RNA knockdown, results in the generation of a complex nucleoplasmic reticulum that depends for its formation on the enzyme CTP:phosphocholine-cytidylyltransferase-alpha (CCT-alpha, also known as choline-phosphate cytidylyltransferase A). This structure can form during interphase, confirming that it is independent of mitosis and therefore not a consequence of disordered nuclear envelope assembly. Serial-section dual-axis electron tomography reveals that these invaginations can take two forms: one in which the inner nuclear membrane infolds alone with an inter membrane space interior, and the other in which an invagination of both nuclear membranes occurs, enclosing a cytoplasmic core. Both types of invagination can co-exist in one nucleus and both are frequently studded with nuclear pore complexes (NPC), which reduces NPC abundance on the nuclear surface.
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