• Open Access

Nuclear lamins: key regulators of nuclear structure and activities

Authors

  • Miron Prokocimer,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Maya Davidovich,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Malka Nissim-Rafinia,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Naama Wiesel-Motiuk,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Daniel Z. Bar,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Rachel Barkan,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Eran Meshorer,

    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
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  • Yosef Gruenbaum

    Corresponding author
    1. Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
      Correspondence to: Yosef GRUENBAUM, Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
      Tel.: 972-2-6585995
      Fax: 972-2-5637848
      E-mail: gru@vms.huji.ac.il
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Correspondence to: Yosef GRUENBAUM, Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Tel.: 972-2-6585995
Fax: 972-2-5637848
E-mail: gru@vms.huji.ac.il

Abstract

  • • The lamin molecule
    • - Domain organization of lamins
    • - Lamins are divided to type A and type B
    • - Post-translational processing of lamin molecules
    • - Lamin molecules in evolution
  • • The supramolecular assembly of lamins
    • - From lamin monomer to lamin dimer
    • - From dimers to filaments
    • - The roles of the different domains in the assembly of lamins
    • - Laminopathic mutations affect lamin filament assembly
    • - Lamin assembly in vivo
  • • Lamin-binding proteins
    • - Lamins, chromatin and epigenesis
    • - Lamin binding to DNA
    • - Lamin binding to chromatin
    • - Lamins affect chromatin organization and epigenesis
    • - Lamins are involved in many nuclear functions
    • - Lamins determine the shape and stiffness of the nucleus
    • - Lamins and DNA replication
    • - Lamins in transcription and splicing
  • • Lamins and aging
    • - Lamins and laminopathies
    • - Mutations in lamins and their associated proteins causing ‘laminopathies’
    • - Animal models for laminopathies
    • - Molecular models for laminopathies
  • • Lamins and stem cells
    • - The Notch pathway
    • - The Wnt/β-catenin pathway
    • - Other pathways
  • • Lamins and cancer
    • - Lamins as biomarkers for cancer
    • - Lamins and cancer regulating pathways
    • - Lamins and cancer related aneuploidy
  • • Lamin and viruses

Abstract

The nuclear lamina is a proteinaceous structure located underneath the inner nuclear membrane (INM), where it associates with the peripheral chromatin. It contains lamins and lamin-associated proteins, including many integral proteins of the INM, chromatin modifying proteins, transcriptional repressors and structural proteins. A fraction of lamins is also present in the nucleoplasm, where it forms stable complexes and is associated with specific nucleoplasmic proteins. The lamins and their associated proteins are required for most nuclear activities, mitosis and for linking the nucleoplasm to all major cytoskeletal networks in the cytoplasm. Mutations in nuclear lamins and their associated proteins cause about 20 different diseases that are collectively called laminopathies’. This review concentrates mainly on lamins, their structure and their roles in DNA replication, chromatin organization, adult stem cell differentiation, aging, tumorogenesis and the lamin mutations leading to laminopathic diseases.

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