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The nucleoskeleton: lamins and actin are major players in essential nuclear functions. | LitMetric

The nucleoskeleton: lamins and actin are major players in essential nuclear functions.

Curr Opin Cell Biol

Northwestern University, Feinberg School of Medicine, Department of Cell and Molecular Biology, 303 East Chicago Avenue, Chicago, IL 60611, USA.

Published: June 2003

AI Article Synopsis

  • The nucleoskeleton consists of structural proteins that support DNA replication, transcription, and various nuclear functions.
  • Type-V intermediate filament proteins, such as lamins and associated proteins, are crucial for these processes alongside actin and its related proteins, emphasizing their roles in chromatin remodeling and mRNA activities.
  • Recent discoveries of proteins that bind both actin and lamin may shed light on the interactions between these nucleoskeletal proteins, helping to explain the connection between genetic defects in these proteins and a growing number of human diseases.

Article Abstract

The nucleoskeleton is composed of many interacting structural proteins that provide the framework for DNA replication, transcription and a variety of other nuclear functions. For example, the type-V intermediate filament proteins, the lamins, and their associated proteins (e.g. Lap2alpha) play important roles in DNA replication and transcription. Furthermore, actin, actin-related proteins and other actin-associated proteins likewise appear to be important in nuclear functions because they are components of chromatin-remodeling complexes and are involved in mRNA synthesis, processing and transport. Newly described nuclear proteins that contain both actin- and lamin-binding domains could be involved in regulating molecular crosstalk between these two types of nucleoskeletal proteins. This range of activities might help to explain why genetic defects in some of the nucleoskeletal proteins contribute to an ever-expanding list of human diseases.

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Source
http://dx.doi.org/10.1016/s0955-0674(03)00050-4DOI Listing

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