Liquid-liquid phase separation: Galectin-3 in nuclear speckles and ribonucleoprotein complexes.

Liquid-liquid phase separation: Galectin-3 in nuclear speckles and ribonucleoprotein complexes.
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DOI:
10.1016/j.yexcr.2023.113571
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发表时间:
2023-06-01
影响因子:
3.7
通讯作者:
Wang, John L.
Wang, John L.
中科院分区:
医学3区
文献类型:
--
作者:
Voss, Patricia G.;Wang, John L.

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Nuclear speckles are subcellular structures originally characterized by punctate immunofluorescence staining of the monoclonal antibody SC35, which recognizes an epitope on SRRM2 (serine/arginine repetitive matrix protein 2) and Sfrs2, a member of the SR (serine/arginine-rich) family of splicing factors. Galectin-3 co-localizes with SC35 in nuclear speckles, which represent one group of nuclear bodies that include the nucleolus, Cajal bodies and gems, paraspeckles, etc. Although they appear to have well-delineated physical boundaries, these nuclear bodies are not membrane-bound structures but represent macromolecular assemblies arising from a phenomenon called liquid-liquid phase separation. There has been much recent interest in liquid phase condensation as a newly recognized mechanism by which a cell can organize and compartmentalize subcellular structures with distinct composition. The punctate/speckled staining of galectin-3 with SC3 demonstrates their co-localization in a phase-separated body in vivo, under conditions endogenous to the cell. The purpose of the present review is to summarize the studies that document three key features of galectin-3 for its localization in liquid phase condensates: (a) an intrinsically disordered domain; (b) oligomer formation for multivalent binding; and (c) association with RNA and ribonucleoprotein complexes.
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