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Nuclear lamins: key regulators of nuclear structure and activities.

Prokocimer M, Davidovich M, Nissim-Rafinia M, Wiesel-Motiuk N, Bar DZ, Barkan R, Meshorer E, Gruenbaum Y - J. Cell. Mol. Med. (2009)

Bottom Line: 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'.

View Article: PubMed Central - PubMed

Affiliation: Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Israel.

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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Schematic view of the nuclear envelope, lamina and chromatin. The inner nuclear membrane (INM) and the outer nuclear membranes (ONM) are joined at the nuclear pore complexes and separated by the nuclear lumen. The ONM and lumen are continuous with the endoplasmic reticulum (ER). Lamins (both A- and B-types) are shown as orange filaments; thicker at the nuclear periphery and thinner filaments in the nucleoplasm. However, the filamentous nature of the lamins, especially within the nucleus, remains hypothetical. Also shown are selected proteins of the INM including LEM-domain and SUN-domain proteins, LAP-1, Nurim and LBR (boudreaux). These proteins represent only a small fraction of proteins of the INM. Also shown few examples of non-integral proteins that interact with lamins or with their associated proteins including actin, HP1, HA95, germ cell-less and BAF. The nucleoplasmic lamins also form specific protein complexes (not shown). INM SUN-domain proteins interact with outer nuclear membrane (ONM) KASH-domain proteins, thus bridging between the nucleus and cytoplasmic structures including, actin (green), tubulin (yellow) and intermediate filament (not shown) networks and the centrosome (MTOC).
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fig03: Schematic view of the nuclear envelope, lamina and chromatin. The inner nuclear membrane (INM) and the outer nuclear membranes (ONM) are joined at the nuclear pore complexes and separated by the nuclear lumen. The ONM and lumen are continuous with the endoplasmic reticulum (ER). Lamins (both A- and B-types) are shown as orange filaments; thicker at the nuclear periphery and thinner filaments in the nucleoplasm. However, the filamentous nature of the lamins, especially within the nucleus, remains hypothetical. Also shown are selected proteins of the INM including LEM-domain and SUN-domain proteins, LAP-1, Nurim and LBR (boudreaux). These proteins represent only a small fraction of proteins of the INM. Also shown few examples of non-integral proteins that interact with lamins or with their associated proteins including actin, HP1, HA95, germ cell-less and BAF. The nucleoplasmic lamins also form specific protein complexes (not shown). INM SUN-domain proteins interact with outer nuclear membrane (ONM) KASH-domain proteins, thus bridging between the nucleus and cytoplasmic structures including, actin (green), tubulin (yellow) and intermediate filament (not shown) networks and the centrosome (MTOC).

Mentions: The many roles of lamins are mediated by interactions with numerous lamin-binding proteins both at the nuclear periphery and in the nucleoplasm (Fig. 3). There is increasingly growing number of mammalian inner nuclear membrane (INM) proteins [36], and most of these proteins probably bind lamins either directly or indirectly. For example, lamins bind in vitro to INM proteins: emerin, MAN-1, lamin B receptor – LBR, lamina-associated polypeptides-1 and -2β (LAP-1, LAP-2β), nesprin-1α, otefin, Young arrest (YA) and SUN-1. Lamins can also bind non-integral proteins including the chromatin proteins histone H2A/H2B dimers, retinoblastoma protein (pRb), barrier-to-autointegration factor (BAF), as well as LAP-2α, sterol response element binding protein (SREBP), Kruppel-like protein (MOK-2), extracellular signal-regulated kinase (ERK)-1/2, c-Fos, nuclear actin, proliferating cell nuclear antigen (PCNA) and proteins of the NPC [reviewed in 37–39].


Nuclear lamins: key regulators of nuclear structure and activities.

Prokocimer M, Davidovich M, Nissim-Rafinia M, Wiesel-Motiuk N, Bar DZ, Barkan R, Meshorer E, Gruenbaum Y - J. Cell. Mol. Med. (2009)

Schematic view of the nuclear envelope, lamina and chromatin. The inner nuclear membrane (INM) and the outer nuclear membranes (ONM) are joined at the nuclear pore complexes and separated by the nuclear lumen. The ONM and lumen are continuous with the endoplasmic reticulum (ER). Lamins (both A- and B-types) are shown as orange filaments; thicker at the nuclear periphery and thinner filaments in the nucleoplasm. However, the filamentous nature of the lamins, especially within the nucleus, remains hypothetical. Also shown are selected proteins of the INM including LEM-domain and SUN-domain proteins, LAP-1, Nurim and LBR (boudreaux). These proteins represent only a small fraction of proteins of the INM. Also shown few examples of non-integral proteins that interact with lamins or with their associated proteins including actin, HP1, HA95, germ cell-less and BAF. The nucleoplasmic lamins also form specific protein complexes (not shown). INM SUN-domain proteins interact with outer nuclear membrane (ONM) KASH-domain proteins, thus bridging between the nucleus and cytoplasmic structures including, actin (green), tubulin (yellow) and intermediate filament (not shown) networks and the centrosome (MTOC).
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Related In: Results  -  Collection

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fig03: Schematic view of the nuclear envelope, lamina and chromatin. The inner nuclear membrane (INM) and the outer nuclear membranes (ONM) are joined at the nuclear pore complexes and separated by the nuclear lumen. The ONM and lumen are continuous with the endoplasmic reticulum (ER). Lamins (both A- and B-types) are shown as orange filaments; thicker at the nuclear periphery and thinner filaments in the nucleoplasm. However, the filamentous nature of the lamins, especially within the nucleus, remains hypothetical. Also shown are selected proteins of the INM including LEM-domain and SUN-domain proteins, LAP-1, Nurim and LBR (boudreaux). These proteins represent only a small fraction of proteins of the INM. Also shown few examples of non-integral proteins that interact with lamins or with their associated proteins including actin, HP1, HA95, germ cell-less and BAF. The nucleoplasmic lamins also form specific protein complexes (not shown). INM SUN-domain proteins interact with outer nuclear membrane (ONM) KASH-domain proteins, thus bridging between the nucleus and cytoplasmic structures including, actin (green), tubulin (yellow) and intermediate filament (not shown) networks and the centrosome (MTOC).
Mentions: The many roles of lamins are mediated by interactions with numerous lamin-binding proteins both at the nuclear periphery and in the nucleoplasm (Fig. 3). There is increasingly growing number of mammalian inner nuclear membrane (INM) proteins [36], and most of these proteins probably bind lamins either directly or indirectly. For example, lamins bind in vitro to INM proteins: emerin, MAN-1, lamin B receptor – LBR, lamina-associated polypeptides-1 and -2β (LAP-1, LAP-2β), nesprin-1α, otefin, Young arrest (YA) and SUN-1. Lamins can also bind non-integral proteins including the chromatin proteins histone H2A/H2B dimers, retinoblastoma protein (pRb), barrier-to-autointegration factor (BAF), as well as LAP-2α, sterol response element binding protein (SREBP), Kruppel-like protein (MOK-2), extracellular signal-regulated kinase (ERK)-1/2, c-Fos, nuclear actin, proliferating cell nuclear antigen (PCNA) and proteins of the NPC [reviewed in 37–39].

Bottom Line: 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'.

View Article: PubMed Central - PubMed

Affiliation: Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Israel.

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.

Show MeSH