LAP2α-binding protein LINT-25 is a novel chromatin-associated protein involved in cell cycle exit

Naetar, Nana; Hutter, Sabine A.; Dorner, D.; Dechat, Thomas; Korbei, Barbara; Gotzmann, Josef; Beug, Hartmut; Foisner, Roland

doi:10.1242/jcs.03390

Cited by 42 publications

(32 citation statements)

References 52 publications

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“…In these cells, we confirmed that LAP2α was progressively down-regulated upon GFP-progerin expression. Since previous studies have revealed that LAP2α is down-regulated in noncycling wildtype cells, including quiescent, senescent, or differentiated cells (Markiewicz et al 2002(Markiewicz et al , 2005Naetar et al 2007), the observed down-regulation of LAP2α in progerin-expressing cells may be a consequence of progerinmediated cell cycle exit. However, LAP2α mRNA downregulation in these cells occurred already at a time point when the cells had no detectable proliferation defects.…”

Section: Discussionmentioning

confidence: 91%

“…Transient (quiescence) or stable (terminal differentiation and senescence) cell cycle exit has also been found to correlate with down-regulation of LAP2α expression and loss of nucleoplasmic lamins (Markiewicz et al 2002(Markiewicz et al , 2005Naetar et al 2007Naetar et al , 2008. We therefore tested whether the observed loss of LAP2α and nucleoplasmic lamins in HGPS cells correlated with progerin-induced proliferation defects.…”

Section: Loss Of Lap2α Precedes Progerin-dependent Proliferation Defementioning

confidence: 99%

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Proliferation of progeria cells is enhanced by lamina-associated polypeptide 2α (LAP2α) through expression of extracellular matrix proteins

et al. 2015

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Lamina-associated polypeptide 2α (LAP2α) localizes throughout the nucleoplasm and interacts with the fraction of lamins A/C that is not associated with the peripheral nuclear lamina. The LAP2α–lamin A/C complex negatively affects cell proliferation. Lamins A/C are encoded by LMNA, a single heterozygous mutation of which causes Hutchinson-Gilford progeria syndrome (HGPS). This mutation generates the lamin A variant progerin, which we show here leads to loss of LAP2α and nucleoplasmic lamins A/C, impaired proliferation, and down-regulation of extracellular matrix components. Surprisingly, contrary to wild-type cells, ectopic expression of LAP2α in cells expressing progerin restores proliferation and extracellular matrix expression but not the levels of nucleoplasmic lamins A/C. We conclude that, in addition to its cell cycle-inhibiting function with lamins A/C, LAP2α can also regulate extracellular matrix components independently of lamins A/C, which may help explain the proliferation-promoting function of LAP2α in cells expressing progerin.

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Section: Discussionmentioning

confidence: 91%

Section: Loss Of Lap2α Precedes Progerin-dependent Proliferation Defementioning

confidence: 99%

Proliferation of progeria cells is enhanced by lamina-associated polypeptide 2α (LAP2α) through expression of extracellular matrix proteins

et al. 2015

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“…These results indicated that terminal differentiation is accompanied by a reorganization of pericentric heterochromatin. It has also been demonstrated that distribution of heterochromatin is dependent of the state of cell proliferation-diffuse nuclear staining of HP1α was characteristic for non-dividing cells (Grigoryev et al 2004;Naetar et al 2007). …”

Section: Discussionmentioning

confidence: 99%

Nuclear organization during in vitro differentiation of porcine mesenchymal stem cells (MSCs) into adipocytes

Stachecka

Walczak

Kociucka

et al. 2017

Histochem Cell Biol

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for further study, a comparative characteristic of the nuclear organization in BM-MSCs and AD-MSCs was performed. Nuclear substructures were visualized by indirect immunofluorescence (nucleoli, nuclear speckles, PML bodies, lamins, and HP1α) or fluorescence in situ hybridization (telomeres) on fixed cells at 0, 3, 5, and 7 days of differentiation. Comprehensive characterization of these structures, in terms of their number, size, dynamics, and arrangement in three-dimensional space of the nucleus, was performed. It was found that during differentiation of porcine MSCs into adipocytes, changes of nuclear organization occurred and concerned: (1) the nuclear size and shape; (2) reduced lamin A/C expression; and (3) reorganization of chromocenters. Other elements of nuclear architecture such as nucleoli, SC-35 nuclear speckles, and telomeres showed no significant changes when compared to undifferentiated and mature fat cells. In addition, the presence of a low number of PML bodies was characteristic of the studied porcine mesenchymal stem cell adipogenesis system. It has been shown that the arrangement of selected components of nuclear architecture was very similar in MSCs derived from different sources, whereas adipocyte differentiation involves nuclear reorganization. This study adds new data on nuclear organization during adipogenesis using the pig as a model organism.

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“…In proliferating cells, LAP2a is essential and sufficient to target and retain a subset of lamins within the nuclear interior (Naetar et al 2007;Naetar et al 2008). Nucleoplasmic lamins are stable, but more mobile than peripheral lamins, suggesting interior lamins assemble differently or bind to chromatin (Moir et al 2000b).…”

Section: Regulation Of Signaling and Proliferation Control By Lamin-bmentioning

confidence: 99%

Lamin-binding Proteins

Wilson¹,

Foisner²

2010

Cold Spring Harbor Perspectives in Biology

235

224

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A-and B-type lamins are the major intermediate filaments of the nucleus. Lamins engage in a plethora of stable and transient interactions, near the inner nuclear membrane and throughout the nucleus. Lamin-binding proteins serve an amazingly diverse range of functions. Numerous inner-membrane proteins help anchor lamin filaments to the nuclear envelope, serving as part of the nuclear "lamina" network that is essential for nuclear architecture and integrity. Certain lamin-binding proteins of the inner membrane bind partners in the outer membrane and mechanically link lamins to the cytoskeleton. Inside the nucleus, lamin-binding proteins appear to serve as the "adaptors" by which the lamina organizes chromatin, influences gene expression and epigenetic regulation, and modulates signaling pathways. Transient interactions of lamins with key components of the transcription and replication machinery may provide an additional level of regulation or support to these essential events.T he eukaryotic cell nucleus is a complex membrane-bounded organelle that houses, organizes, and regulates the genome. The nucleus is structurally organized into functional domains, one of which is the nuclear envelope (NE). The NE has two concentric membranes, named the "inner" and "outer" nuclear membranes (INM and ONM, respectively). These membranes are separated by a 30-50 nm lumen, and fuse to form holes ( pores) occupied by nuclear pore complexes (NPCs), which mediate active and passive movement of molecules between the cytoplasm and nucleoplasm (Gruenbaum et al. 2005;Stewart et al. 2007). The NE and its lumen are continuous with the endoplasmic reticulum (ER) and share many ER functions. However, the INM and ONM are also each structurally and functionally unique, because of specific enrichments for distinct integral membrane proteins Schirmer and Foisner 2007). In mammals, the INM in particular appears to be populated by over 50 different membrane proteins, most of which are uncharacterized. Among characterized INM proteins, most can bind directly to A-or B-type lamins, or both.A-and B-type lamins polymerize to form separate networks of nuclear intermediate filaments that concentrate near the INM in metazoans (Dechat et al. 2008). Many INM proteins are localized by binding directly or indirectly to lamin filaments. This network of filaments and

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LAP2α-binding protein LINT-25 is a novel chromatin-associated protein involved in cell cycle exit

Cited by 42 publications

References 52 publications

Proliferation of progeria cells is enhanced by lamina-associated polypeptide 2α (LAP2α) through expression of extracellular matrix proteins

Proliferation of progeria cells is enhanced by lamina-associated polypeptide 2α (LAP2α) through expression of extracellular matrix proteins

Nuclear organization during in vitro differentiation of porcine mesenchymal stem cells (MSCs) into adipocytes

Lamin-binding Proteins

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