2009
DOI: 10.1002/jcp.21807
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A‐type lamins and signaling: The PI 3‐kinase/Akt pathway moves forward

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 estab… Show more

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Cited by 41 publications
(34 citation statements)
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“…The nucleolus, which lacks lamins, is externally scaffolded by lamin B1, which binds to nucleophosmin and is required for dynamic changes in nucleolar structure (Martin et al, 2009). A-type lamins determine the shape and mechanical stiffness of the nucleus (Dahl et al, 2008) and also influence signaling and gene regulation, for example, by providing binding sites for regulatory proteins, including PKC, Fos and MOK2 (Zastrow et al, 2004;Gonzalez et al, 2008;Gruenbaum et al, 2005;Marmiroli et al, 2009;Harper et al, 2009). A-type lamins contribute to the control of cell proliferation by interacting with LAP2, retinoblastoma protein (Rb) and inhibitor of growth protein 1 (ING1) (Johnson et al, 2004;Dorner et al, 2007;Han et al, 2008;Naetar and Foisner, 2009).…”
mentioning
confidence: 99%
“…The nucleolus, which lacks lamins, is externally scaffolded by lamin B1, which binds to nucleophosmin and is required for dynamic changes in nucleolar structure (Martin et al, 2009). A-type lamins determine the shape and mechanical stiffness of the nucleus (Dahl et al, 2008) and also influence signaling and gene regulation, for example, by providing binding sites for regulatory proteins, including PKC, Fos and MOK2 (Zastrow et al, 2004;Gonzalez et al, 2008;Gruenbaum et al, 2005;Marmiroli et al, 2009;Harper et al, 2009). A-type lamins contribute to the control of cell proliferation by interacting with LAP2, retinoblastoma protein (Rb) and inhibitor of growth protein 1 (ING1) (Johnson et al, 2004;Dorner et al, 2007;Han et al, 2008;Naetar and Foisner, 2009).…”
mentioning
confidence: 99%
“…As SHIP2 is part of the lamin interactome, it is possible that S132 phosphorylation could influence lamin nuclear function and perhaps related laminopathies [55].…”
Section: W Elong Edimo Et Almentioning
confidence: 99%
“…To date, some of the perturbations observed in the various signaling pathways, including MAPK, pRb, MyoD, Wnt-β catenin and TGFβ (transforming growth factor β), have been connected to laminopathic muscular dystrophies [62][63]. The mammalian family of mitogen-activated protein kinases (MAPKs) are serine-threonine kinases that mediate the intracellular signaling associated with a variety of cellular activities.…”
Section: Muscular Dystrophymentioning
confidence: 99%
“…Some new concepts have been published, based on the interaction of lamins with a wide spectrum of diverse proteins and on the mechanism by which lamin defects might alter these interactions to cause disease. Lamins not only interact with each other but also interact and modulate function or determine the location of key proteins of the nuclear membranes (emerin, nesprin, LBR, LAP, MAN1), LINC complex (SUN proteins), nuclear pore complex proteins (Nup153, Nup53), transcription factors (SREBP1, MOK2, pRb, c-Fos, Oct-1), nucleoplasmic proteins (BAF, LAP2α), proteins associated with signal transduction pathways (PKCα, PP1, PP2), DNA and chromatin (H2A, H2B histone dimers, heterochromatin protein-1) [for a review see 63,121]. It should be considered that the formation of a definite complex must be directed by different signaling events.…”
Section: Tissue Selective Phenotyphesmentioning
confidence: 99%
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