The Nuclear Lamina and Its Functions in the Nucleus

Gruenbaum, Yosef; Goldman, Robert D.; Meyuhas, Ronit; Mills, Erez; Margalit, Ayelet; Fridkin, Alexandra; Dayani, Yaron; Prokocimer, Miron; Enosh, Avital

doi:10.1016/s0074-7696(03)01001-5

Cited by 207 publications

(182 citation statements)

References 322 publications

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“…Supporting these data, we found that Dp71, βdystroglycan and β-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. Because lamin B1 is a structural component of the nuclear matrix that facilitates the interaction between chromatin and the inner nuclear membrane [27] and actin is a component of several mammal chromatin-remodeling complexes [44], the association of Dp71 and some DAPC members with those proteins might indicate that they work as scaffolding proteins involved in nuclear architecture. Additional biochemical studies are necessary to establish whether the interaction between DAPC components and actin and lamin B1 is direct or due to an association within the context of a larger nuclear matrix complex.…”

Section: Discussionmentioning

confidence: 99%

“…Dp71d and Dp71f protein isoforms are expressed in HeLa cells; Dp71f distributes exclusively in the cytoplasm, whereas Dp71d accumulates mainly in the nuclear compartment. the other hand, lamin B1, a nuclear matrix-associated protein [27], was used as nuclear marker. As expected, the vinculin (135kDa) and calnexin (90kDa) bands were found exclusively in the cytosolic fraction whereas the lamin B1 band (68kDa) was absent in the cytosolic fraction but present in the nuclear extract (Fig.…”

Section: Expression and Subcellular Localization Of Endogenous Dp71 Pmentioning

confidence: 99%

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Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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, et al.. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix.. Experimental Cell Research, Elsevier, 2006, 312 (16) ABSTRACT: Dystrophin is an essential component in the assembly and maintenance of the dystrophinassociated protein complex (DAPC), which includes members of the dystroglycan, syntrophin, sarcoglycan and dystrobrevin protein families. Distinctive complexes have been described in the cell membrane of different tissues and cultured cells. In this work, we report the identification and characterization of a novel DAPC present in the nuclei of HeLa cells, which contains dystrophin Dp71 as a key component. Using confocal microscopy and cell fractionation analyses, we found the presence of Dp71, β-sarcoglycan, β-dystroglycan, α-and β-syntrophin, α1-and β-dystrobrevin and nNOS in the nuclei of HeLa cells. Furthermore, we demonstrated by coimmunoprecipitation experiments that most of these proteins form a complex in the nuclear compartment. Next, we analyze the possible association of the nuclear DAPC with the nuclear matrix. We found the presence of Dp71, β-dystroglycan, nNOS, β-sarcoglycan, α/β syntrophin, α1-dystrobrevin and β-dystrobrevin in the nuclear matrix protein fractions and in situ nuclear matrix preparations from HeLa cells. Moreover, we found that Dp71, β-dystroglycan and β-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. The association of members of the nuclear DAPC with the nuclear matrix indicates that they may work as scaffolding proteins involved in nuclear architecture.

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Section: Discussionmentioning

confidence: 99%

Section: Expression and Subcellular Localization Of Endogenous Dp71 Pmentioning

confidence: 99%

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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“…The localization of L1 proteins is reminiscent of that of the nuclear lamina (Nickerson et al, 1997;see Gruenbaum et al, 2003 for review). A wealth of evidence indicates the essential role of lamin proteins, and the nuclear lamina structure which they form, in control of fundamental functions, including the organization and positioning of active and nonexpressed chromatin, gene regulation, nuclear architecture and differentiation (reviewed by Goldman et al, 2002;Gruenbaum et al, 2003Gruenbaum et al, , 2005. It is tempting to speculate that L1-encoded proteins, especially L1-RT, participate in or interact with the nuclear lamina structure and, as such, exert their regulatory function on gene expression.…”

Section: Roles Of Line-1 and Herv-k In Tumorigenesis E Oricchio Et Almentioning

confidence: 99%

Distinct roles for LINE-1 and HERV-K retroelements in cell proliferation, differentiation and tumor progression

et al. 2007

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Transformed cells express high levels of non-telomeric reverse-transcriptase (RT) activity of retrotransposon and endogenous retrovirus origin. We previously reported that RT inhibition, either pharmacological or through transient silencing of RT-encoding LINE-1 (L1) elements by RNA interference (RNAi), reduced proliferation, induced differentiation and reprogrammed gene expression in human tumorigenic cell lines. Moreover, the antiretroviral drug efavirenz antagonized tumor progression in animal models in vivo. To get insight into the role of retroelements in tumorigenesis, we have now produced two cell lines derived from A-375 melanoma, in which the expression of either L1 retrotransposon, or HERV-K endogenous retrovirus, was stably suppressed by RNAi. Compared to the parental A-375 cell line, cells with stably interfered L1 expression show a lower proliferation rate, a differentiated morphology and lower tumorigenicity when inoculated in nude mice. L1 silencing modulates expression of several genes and, unexpectedly, also downregulates HERV-K expression. In HERV-K interfered cells, instead, L1 expression was unaffected, and cell proliferation and differentiation remained unchanged compared to parental A-375 cells. In vivo, however, their tumorigenic potential was found to be reduced after inoculation in nude mice. These results suggest that L1 and HERV-K play specific and distinct roles in cell transformation and tumor progression.

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“…Current concepts of the nuclear envelope [5][6][7][8][9][10] visualize a multi-tiered structure with a specialized inner nuclear membrane contiguous via nuclear pores to the outer nuclear membrane-endoplasmic reticulum system, but otherwise separated by a perinuclear space. Internal to the inner nuclear membrane is a meshwork layer of intermediate filaments (lamins) interacting directly or indirectly with an underlying layer of peripheral heterochromatin.…”

Section: Introductionmentioning

confidence: 99%

Granulocytic nuclear differentiation of lamin B receptor–deficient mouse EPRO cells

Zwerger

Herrmann

Gaines

et al. 2008

Experimental Hematology

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Objective-Lamin B receptor (LBR) is an integral protein of the inner nuclear membrane. Recent studies have demonstrated that genetic deficiency of LBR during granulopoiesis results in hypolobulation of the mature neutrophil nucleus, as observed in human Pelger-Huët anomaly (PHA) and mouse ichthyosis (ic). In this study we have utilized differentiated promyelocytes (EPRO cells) that were derived from the bone marrow of homozygous and heterozygous ichthyosis mice to examine changes to the expression of nuclear envelope proteins and heterochromatin structure that result from deficient LBR expression.Materials and Methods-Wildtype (+/+), heterozygous (+/ic) and homozygous (ic/ic) granulocytic forms of EPRO cells were analyzed for the expression of multiple lamins and inner nuclear envelope proteins by immunostaining and immunoblotting techniques. The heterochromatin architecture was also examined by immunostaining for histone lysine methylation.Results-Wildtype (+/+) and heterozygous (+/ic) granulocytic forms revealed ring-shaped nuclei and contained LBR within the nuclear envelope; ic/ic granulocytes exhibited smaller ovoid nuclei devoid of LBR. The pericentric heterochromatin of undifferentiated and granulocytic ic/ic cells was condensed into larger spots and shifted away from the nuclear envelope, compared to +/+ and +/ic cell forms. Lamin A/C, which is normally not present in mature granulocytes, was significantly elevated in LBR-deficient EPRO cells.Conclusions-Our observations suggest roles for LBR during granulopoiesis which may involve augmenting nuclear membrane growth, facilitating compartmentalization of heterochromatin and promoting down-regulation of lamin A/C expression. Category Granulopoiesis

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The Nuclear Lamina and Its Functions in the Nucleus

Cited by 207 publications

References 322 publications

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Distinct roles for LINE-1 and HERV-K retroelements in cell proliferation, differentiation and tumor progression

Granulocytic nuclear differentiation of lamin B receptor–deficient mouse EPRO cells

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