Loss of a DNA binding site within the tail of prelamin A contributes to altered heterochromatin anchorage by progerin

Bruston, Francine; Delbarre, Erwan; Östlund, Cecilia; Worman, Howard J.; Buendia, Brigitte; Duband-Goulet, Isabelle

doi:10.1016/j.febslet.2010.05.032

Cited by 46 publications

(42 citation statements)

References 24 publications

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“…Several groups have shown that A-type and B-type lamins form distinct but connected networks [24,33–35]. These different subdomains of the lamina have specific roles in nuclear structure, anchorage of partners, binding to chromatin, chromatin organization and gene regulation [36,37]. Our findings complement these previous studies by illustrating the specificity of functions played by Atype and B-type lamins.…”

Section: Discussionsupporting

confidence: 85%

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

Duband-Goulet

Woerner

Gasparini

et al. 2011

Experimental Cell Research

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Lamins A and C are nuclear intermediate filament proteins expressed in most differentiated somatic cells. Previous data suggested that prelamin A, the lamin A precursor, accumulates in some lipodystrophy syndromes caused by mutations in the lamin A/C gene, and binds and inactivates the sterol regulatory element binding protein 1 (SREBP1). Here we show that, in vitro, the tail regions of prelamin A, lamin A and lamin C bind a polypeptide of SREBP1. Such interactions also occur in HeLa cells, since expression of lamin tail regions impedes nucleolar accumulation of the SREBP1 polypeptide fused to a nucleolar localization signal sequence. In addition, the tail regions of A-type lamin variants that occur in Dunnigan-type familial partial lipodystrophy of (R482W) and Hutchison Gilford progeria syndrome (Δ607–656) bind to the SREBP1 polypeptide in vitro, and the corresponding FLAG-tagged full-length lamin variants co-immunoprecipitate the SREBP1 polypeptide in cells. Overexpression of wild-type A-type lamins and variants favors SREBP1 polypeptide localization at the intranuclear periphery, suggesting its sequestration. Our data support the hypothesis that variation of A-type lamin protein level and spatial organization, in particular due to disease-linked mutations, influences the sequestration of SREBP1 at the nuclear envelope and thus contributes to the regulation of SREBP1 function.

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Section: Discussionsupporting

confidence: 85%

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

Duband-Goulet

Woerner

Gasparini

et al. 2011

Experimental Cell Research

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“…In fact, modulation of chromatin remodelling by prelamin A could be a fine tool to modify expression of large groups of genes, as occurs during development, cell differentiation or aging. This hypothesis is strongly supported by data obtained in the study of syndromic laminopathies and lipodystrophies, which are characterized by prelamin A accumulation [18,[40][41][42].…”

Section: Prelamin A-dependent Mechanismsmentioning

confidence: 54%

Prelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells

Lattanzi

2011

Biochemical Society Transactions

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Prelamin A is the precursor protein of lamin A, a major constituent of the nuclear lamina in higher eukaryotes. Increasing attention to prelamin A processing and function has been given after the discovery, from 2002 to 2004, of diseases caused by prelamin A accumulation. These diseases, belonging to the group of laminopathies and mostly featuring LMNA mutations, are characterized, at the clinical level, by different degrees of accelerated aging, and adipose tissue, skin and bone abnormalities. The outcome of studies conducted in the last few years consists of three major findings. First, prelamin A is processed at different rates under physiological conditions depending on the differentiation state of the cell. This means that, for instance, in muscle cells, prelamin A itself plays a biological role, besides production of mature lamin A. Secondly, prelamin A post-translational modifications give rise to different processing intermediates, which elicit different effects in the nucleus, mostly by modification of the chromatin arrangement. Thirdly, there is a threshold of toxicity, especially of the farnesylated form of prelamin A, whose accumulation is obviously linked to cell and organism senescence. The present review is focused on prelamin A-mediated nuclear envelope modifications that are upstream of chromatin dynamics and gene expression mechanisms regulated by the lamin A precursor.

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“…Receptor for Wnt7 Frizzled7 (Fzd7) is expressed in hypaxial part of the somite while Fzd1 and Fzd6 (receptors for Wnt1/6) are expressed in epaxial domain. Wnt1 in epaxial domain acts through canonical pathway which leads to expression of Myf5 while Wnt7 (Fzd7) signaling induces MyoD expression through PKC pathway [34]. Thus the differentiation of muscle progenitor cells in hypaxial domain and epaxial domain is regulated diifferently, via different muscle-specific transcription factors.…”

Section: Prenatal Myogenesis and Its Regulatory Mechanismsmentioning

confidence: 99%

Muscle development, regeneration and laminopathies: how lamins or lamina-associated proteins can contribute to muscle development, regeneration and disease

Dubińska–Magiera

Zaremba-Czogalla

Rzepecki

2012

Cell. Mol. Life Sci.

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The aim of this review article is to evaluate the current knowledge on associations between muscle formation and regeneration and components of the nuclear lamina. Lamins and their partners have become particularly intriguing objects of scientific interest since it has been observed that mutations in genes coding for these proteins lead to a wide range of diseases called laminopathies. For over the last 10 years, various laboratories worldwide have tried to explain the pathogenesis of these rare disorders. Analyses of the distinct aspects of laminopathies resulted in formulation of different hypotheses regarding the mechanisms of the development of these diseases. In the light of recent discoveries, A-type lamins—the main building blocks of the nuclear lamina—together with other key elements, such as emerin, LAP2α and nesprins, seem to be of great importance in the modulation of various signaling pathways responsible for cellular differentiation and proliferation.

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Loss of a DNA binding site within the tail of prelamin A contributes to altered heterochromatin anchorage by progerin

Cited by 46 publications

References 24 publications

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

Prelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells

Muscle development, regeneration and laminopathies: how lamins or lamina-associated proteins can contribute to muscle development, regeneration and disease

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