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A-type lamins and signaling: The PI 3-kinase/Akt pathway moves forward

Authors

  • Sandra Marmiroli,

    Corresponding author
    1. Department of Anatomy and Histology and CIPro Proteomics Centre, University of Modena and Reggio Emilia, Modena, Italy
    2. I.G.M.-CNR, Unit of Bologna, Bologna, Italy
    • Department of Anatomy and Histology and CIPro Proteomics Centre, University of Modena and Reggio Emilia, Via Del Pozzo 71, I-41100 Modena, I.G.M.-CNR, Unit of Bologna, c/o IOR, via di Barbiano, I-40136 Bologna, Italy.
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  • Jessika Bertacchini,

    1. Department of Anatomy and Histology and CIPro Proteomics Centre, University of Modena and Reggio Emilia, Modena, Italy
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  • Francesca Beretti,

    1. Department of Anatomy and Histology and CIPro Proteomics Centre, University of Modena and Reggio Emilia, Modena, Italy
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  • Vittoria Cenni,

    1. I.G.M.-CNR, Unit of Bologna, Bologna, Italy
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  • Marianna Guida,

    1. Department of Anatomy and Histology and CIPro Proteomics Centre, University of Modena and Reggio Emilia, Modena, Italy
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  • Anto De Pol,

    1. Department of Anatomy and Histology and CIPro Proteomics Centre, University of Modena and Reggio Emilia, Modena, Italy
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  • Nadir M. Maraldi,

    1. I.G.M.-CNR, Unit of Bologna, Bologna, Italy
    2. Laboratory of Cellular Biology and Electron Microscopy, Bologna, Italy
    3. Department of Human Anatomical Sciences, University of Bologna, Bologna, Italy
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  • Giovanna Lattanzi

    1. I.G.M.-CNR, Unit of Bologna, Bologna, Italy
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Abstract

Lamin A/C is a nuclear lamina constituent mutated in a number of human inherited disorders collectively referred to as laminopathies. The occurrence and significance of lamin A/C interplay with signaling molecules is an old question, suggested by pioneer studies performed in vitro. However, this relevant question has remained substantially unanswered, until data obtained in cellular and organismal models of laminopathies have indicated two main aspects of lamin A function. The first aspect is that lamins establish functional interactions with different protein platforms, the second aspect is that lamin A/C activity and altered function may elicit different effects in different cells and tissue types and even in different districts of the same tissue. Both these observations strongly suggest that signaling mechanisms targeting lamin A/C or its binding partners may regulate such a plastic behavior. A number of very recent data show involvement of kinases, as Akt and Erk, or phosphatases, as PP1 and PP2, in lamin A-linked cellular mechanisms. Moreover, altered activation of signaling in laminopathies and rescue of the pathological phenotype in animal models by inhibitors of signaling pathways, strongly suggest that signaling effectors related to lamin A/C may be implicated in the pathogenesis of laminopathies and may represent targets of therapeutic intervention. In face of such an open perspective of basic and applied research, we review current evidence of lamin A/C interplay with signaling molecules, with particular emphasis on the lamin A-Akt interaction and on the biological significance of their relationship. J. Cell. Physiol. 220: 553–561, 2009. © 2009 Wiley-Liss, Inc.

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