![]() ![]() Studying the role of NS involves visualizing them with a fluorescently tagged factor that localizes to NS, or the use of antibodies that show specific staining of NS. ![]() ![]() NS have been shown to be involved in replication of herpes simplex virus ( Chang et al., 2011), processing and trafficking of Influenza A virus mRNA ( Mor et al., 2016), detaining repetitive RNA originating from the transcription of repeat expanded loci that trigger Huntington's disease, spinocerebellar ataxia and dentatorubral–pallidoluysian atrophy ( Urbanek et al., 2016), but also repetitive RNA from artificial constructs that produce RNA capable of phase-separation in vitro ( Jain and Vale, 2017). Despite their prevalence, the function of NS remains largely unknown, although they have been proposed to act as reservoirs for splicing factors, and association with NS have been shown to correlate with enhanced transcription and RNA-processing ( Chen and Belmont, 2019 Galganski et al., 2017). Under normal conditions, they appear as irregularly shaped, dynamic structures that show hallmarks of phase-separated condensates, such as fusion and deformation under pressure in living cells ( Chen and Belmont, 2019 Zhang et al., 2016). Nuclear speckles (NS) are membraneless nuclear bodies ( Banani et al., 2017 Shin and Brangwynne, 2017) in the interchromatin-space of the nucleus that contain high concentrations of RNA-processing and some transcription factors but are devoid of DNA ( Spector and Lamond, 2011). These newly discovered core proteins could therefore further our understanding of the role NS play in disease. Nuclear speckles have been associated with certain viral infections, and seem to help prevent the onset of diseases such as Huntington’s and spinocerebellar ataxia. This suggests that SRMM2 and SON make up the scaffold that holds the proteins in NS together. found that depleting SON and SRRM2 from human cells caused other proteins associated with the NS to diffuse away from their territories and become dispersed within the nucleus. Studying the evolutionary history of SRRM2 led to the identification of another protein with similar properties called SON. discovered that although the structure and sequence of SRMM2 varies between different animal species, a small region of this protein remained unchanged throughout evolution. The analysis revealed that SC35 attaches to certain parts of a large, flexible protein called SRRM2. ![]() studied NS in human cells grown in the lab. However, it was unclear which parts of the NS this marker binds to. Typically, researchers visualize NS using a substance called SC35 which targets specific sites in these structures. Although NS were discovered over a century ago, little is known about their scaffold proteins, making it difficult to understand the precise role of these speckles. Structures like NS often contain a number of different factors held together by a core group of proteins known as a scaffold. One of the first nuclear territories to be identified were granular looking structures named Nuclear Speckles (or NS for short), which are thought to help process RNA before it leaves the nucleus. However, the contents of the nucleus are not randomly arranged, and these proteins are often clustered into specialized areas where they perform their designated roles. Inside the nucleus, DNA is tightly packed together with proteins that can read the cell’s genetic code and convert into the RNA molecules needed to build proteins. Most cells store their genetic material inside a compartment called the nucleus, which helps to separate DNA from other molecules in the cell. ![]()
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