Nuclear structure/gene expression interrelationships

Stein, Gary S.; Wijnen, André J. van; Montecino, Martín; Lian, Jane B.

doi:10.1002/(sici)1097-4652(199911)181:2<240::aid-jcp6>3.0.co;2-k

Cited by 11 publications

(2 citation statements)

References 120 publications

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“…The simplest interpretation of such data is that the cytoplasmic IFs actively stretch the nuclear envelope and/or the arrangement of the underlying heterochromatin. Such deformation has been correlated with intranuclear events such as gene expression and chromosomal arrangement (Chen et al, 1997;Croft et al, 1999;Lelievre and Bissell, 1998;review by Maxwell and Hendzel, 2001;Stein et al, 1999Stein et al, , 1998.…”

Section: Desmin's Role In Nuclear Positioning and Deformationmentioning

confidence: 99%

Structural and Functional Roles of Desmin in Mouse Skeletal Muscle during Passive Deformation

Shah¹,

Davis²,

Weisleder

et al. 2004

Biophysical Journal

122

114

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Mechanical interactions between desmin and Z-disks, costameres, and nuclei were measured during passive deformation of single muscle cells. Image processing and continuum kinematics were used to quantify the structural connectivity among these structures. Analysis of both wild-type and desmin-null fibers revealed that the costamere protein talin colocalized with the Z-disk protein alpha-actinin, even at very high strains and stresses. These data indicate that desmin is not essential for mechanical coupling of the costamere complex and the sarcomere lattice. Within the sarcomere lattice, significant differences in myofibrillar connectivity were revealed between passively deformed wild-type and desmin-null fibers. Connectivity in wild-type fibers was significantly greater compared to desmin-null fibers, demonstrating a significant functional connection between myofibrils that requires desmin. Passive mechanical analysis revealed that desmin may be partially responsible for regulating fiber volume, and consequently, fiber mechanical properties. Kinematic analysis of alpha-actinin strain fields revealed that knockout fibers transmitted less shear strain compared to wild-type fibers and experienced a slight increase in fiber volume. Finally, linkage of desmin intermediate filaments to muscle nuclei was strongly suggested based on extensive loss of nuclei positioning in the absence of desmin during passive fiber loading.

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Section: Desmin's Role In Nuclear Positioning and Deformationmentioning

confidence: 99%

Structural and Functional Roles of Desmin in Mouse Skeletal Muscle during Passive Deformation

Shah¹,

Davis²,

Weisleder

et al. 2004

Biophysical Journal

122

114

View full text Add to dashboard Cite

show abstract

“…Advances in light and electron microscopy techniques, coupled with the localization of individual proteins has revealed that the nucleus is an organized structure and many nuclear proteins have speci®c sub-nuclear addresses [reviewed in Cardoso and Leonhardt, 1998;Lamond and Earnshaw, 1998]. The nuclear matrix, the non-chromatin nuclear scaffolding, is an integral player in the organization of structure and function in the nucleus performing regulatory roles in DNA replication, transcription, and RNA processing by locally concentrating regulatory factors [reviewed in Strouboulis and Wolffe, 1996;Cardoso and Leonhardt, 1998;Stein et al, 1999]. In cancerous cells, there are marked changes in the structure, size and internal organization of the nuclei [reviewed in Nickerson, 1998].…”

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confidence: 99%

Alterations in subnuclear trafficking of nuclear regulatory factors in acute leukemia

Meyers¹,

Hiebert²

2000

J. Cell. Biochem.

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The nuclear matrix plays an important role in the functional organization of the nucleus in part by locally concentrating regulatory factors involved in nucleic acid metabolism. A number of nuclear regulatory proteins initially identi®ed due to their involvement in human cancer are localized to discrete nuclear matrix-attached foci and correct nuclear partitioning likely plays a role in their function. Two such examples are promyelocytic leukemia (PML) and acute myelogenous leukemia-1 (AML-1; Runx1). PML, the target of the t(15;17) in acute PML, is localized to PML nuclear bodies (also termed Nuclear Domain 10 and PML oncogenic domains), a nuclear matrix-associated body whose function appears to be quite complex, with probable roles in cancer, apoptosis, and in acute viral infections. In t(15;17)-containing leukemic cells, the PML nuclear bodies are disrupted, but reform when the leukemic cells are induced to differentiate in the presence of all-trans retinoic acid. AML1 (RUNX1) is a key regulator of hematopoietic differentiation and AML1 proteins are found in nuclear compartments that re¯ect their roles in transcriptional activation and repression. The t(8;21), associated with AML, results in a chimeric transcription factor, AML-1/ETO (eight twenty one), that remains attached to the nuclear matrix through targeting signals contained in the ETO protein. When co-expressed, ETO and AML-1/ETO co-localize to a nuclear compartment distinct from that of AML1 or PML nuclear bodies. Interestingly, enforced expression of ETO or AML-1/ETO changes the average number of PML nuclear bodies per cell. Thus, chromosomal translocations involving AML1 result in altered nuclear traf®cking of the transcription factor as well as other changes to the nuclear architecture.In the past 30 years the view of the nucleus as composed of nucleoplasm and chromatin has evolved as ordered structures such as the nuclear matrix were identi®ed [Berezney and Coffey, 1974]. Advances in light and electron microscopy techniques, coupled with the localization of individual proteins has revealed that the nucleus is an organized structure and many nuclear proteins have speci®c sub-nuclear addresses [reviewed in Cardoso and Leonhardt, 1998;Lamond and Earnshaw, 1998]. The nuclear matrix, the non-chromatin nuclear scaffolding, is an integral player in the organization of structure and function in the nucleus performing regulatory roles in DNA replication, transcription, and RNA processing by locally concentrating regulatory factors [reviewed in Strouboulis and Wolffe, 1996;Cardoso and Leonhardt, 1998;Stein et al., 1999]. In cancerous cells, there are marked changes in the structure, size and internal organization of the nuclei [reviewed in Nickerson, 1998]. These changes may be the result of direct changes in the nuclear matrix and/or sub-nuclear localization of regulatory proteins. Because nucleic acid metabolism is organized through DNA and protein contacts with the nuclear matrix, disruption in nuclear architecture can affect the assembly of regulatory ...

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pRb2/p130 and p107 control cell growth by multiple strategies and in association with different compartments within the nucleus*

Zini¹,

Trimarchi²,

Claudio

et al. 2001

Journal Cellular Physiology

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It has been recently reported that retinoblastoma family proteins suppress cell growth by regulating not only E2F-dependent mRNA transcription but also rRNA and tRNA transcription and, through HDAC1 recruitment, chromatin packaging. In the present study we report data showing that these various control strategies are correlated, at least in part, with nuclear compartmentalization of retinoblastoma proteins. In a first series of experiments, we showed that pRb2/p130 and p107 are not evenly distributed within the nucleus and that cell cycle-dependent binding with E2F4 changes also as a function of their subnuclear localization. Namely, in the nucleoplasm pRb2/p130-E2F4 complexes are more numerous during G0/G1 while in the nucleolus they increase in S phase. Partially different functions for p107 are suggested since p107-E2F4 complexes in the nucleoplasm are more numerous is S phase with respect to G0/G1 and no cell cycle change is observed in the nucleolus. In a second series of experiments we showed that pRb2/p130, p107, E2F4, and pRb2/p130-HDAC1 complexes are all inner nuclear matrix-associated proteins and localize to sites different from pRb/p105 ones. We provide further evidence of multiple and partially distinct retinoblastoma protein family functional roles during cell cycle. Moreover, our data support emerging evidence for functional interrelationships between nuclear structure and gene expression.

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Nuclear structure/gene expression interrelationships

Cited by 11 publications

References 120 publications

Structural and Functional Roles of Desmin in Mouse Skeletal Muscle during Passive Deformation

Structural and Functional Roles of Desmin in Mouse Skeletal Muscle during Passive Deformation

Alterations in subnuclear trafficking of nuclear regulatory factors in acute leukemia

pRb2/p130 and p107 control cell growth by multiple strategies and in association with different compartments within the nucleus*

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