Histone Acetyltransferase hALP and Nuclear Membrane Protein hsSUN1 Function in De-condensation of Mitotic Chromosomes

Chi, Ya‐Hui; Haller, Kerstin; Péloponèse, Jean-Marie; Jeang, Kuan‐Teh

doi:10.1074/jbc.m703098200

Cited by 104 publications

(89 citation statements)

References 60 publications

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“…The N terminus of Sun1 is required for its inner nuclear membrane localization (Chi et al, 2007;Liu et al, 2007), while the SUN C terminus connects to the cytoskeleton through nesprin (Padmakumar et al, 2005). To investigate the physiological function of mammalian Sun1, we generated a Sun1 knockout mouse by targeted deletion of exons 10 and 11 (amino acids 344 to 408) that correspond to the transmembrane domains.…”

Section: Construction Of Sun1mentioning

confidence: 99%

“…Conversely, the Caenorhabditis elegans SUNdomain protein Unc-84 is required for nuclear migration and anchorage (Lee et al, 2002). In mammalian cells, the N terminus of Sun1 targets the protein to the inner nuclear membrane (Chi et al, 2007), while the C terminus of the protein connects to cytoplasmic actin through a direct interaction with Nesprin (Crisp et al, 2006;Padmakumar et al, 2005). In somatic cells, human SUN1 has been described to be one of the early INM factors that associate with segregated daughter chromosomes in anaphase, participating in post-mitotic chromatin de-condensation by recruiting a membraneassociated histone acetyl transferase, hALP (Chi et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Requirement for Sun1 in the expression of meiotic reproductive genes and piRNA

et al. 2009

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The inner nuclear envelope (NE) proteins interact with the nuclear lamina and participate in the architectural compartmentalization of chromosomes. The association of NE proteins with DNA contributes to the spatial rearrangement of chromosomes and their gene expression. Sun1 is an inner nuclear membrane (INM) protein that locates to telomeres and anchors chromosome movement in the prophase of meiosis. Here, we have created Sun1 -/-mice and have found that these mice are born and grow normally but are reproductively infertile. Detailed molecular analyses showed that Sun1 -/-P14 testes are repressed for the expression of reproductive genes and have no detectable piRNA. These findings raise a heretofore unrecognized role of Sun1 in the selective gene expression of coding and non-coding RNAs needed for gametogenesis.

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Section: Construction Of Sun1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Requirement for Sun1 in the expression of meiotic reproductive genes and piRNA

et al. 2009

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“…[1][2][3][4] Mammalian SUN proteins are encoded by at least 5 genes, SUN1»5. SUN1 and SUN2 are widely expressed in mammalian somatic cells.…”

Section: Introductionmentioning

confidence: 99%

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration

Nishioka

Imaizumi

Imada

et al. 2016

Nucleus

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The LINC complex is a multifunctional protein complex that is involved in various processes at the nuclear envelope, such as nuclear migration, mechanotransduction and chromatin tethering in the meiotic phase. However, it remains unknown how these functions are regulated in different cell contexts. An inner nuclear membrane component of the LINC complex, SUN1, is ubiquitously expressed. The human SUN1 gene produces over 10 variants by alternative splicing. Although functions of SUN1 are relatively well characterized, functional differences among SUN1 splice variants are poorly characterized. LINC complex components are associated with a wide range of human diseases; therefore, it is important to understand the functional diversity among SUN1 splice variants. Here, we identified a novel human SUN1 splice variant, SUN1_888. overexpression of the SUN1 splice variants, SUN1_888 or SUN1_785, but not the predominant isoform, SUN1_916, activated directional cell migration. Knockdown of SUN1_888 suppressed cell migration; in contrast depletion of SUN1_916 activated cell migration. In addition, all of investigated SUN1 splicing variants rescued cell migration in SUN1 knock out cell. These results indicate that redundant and non-redundant functions of SUN1 splice variant in directional cell migration and suggest that variable LINC complexes with distinct task may exit. Furthermore, in contrast to previous studies, we showed association between SUN1 and B-type lamins. Interestingly, B-type lamin preferentially interacts with SUN1 but not SUN2. These results suggest that tissue-specific SUN1 variants variably interact with nucleoplasmic partners and allow variable assembly of LINC complexes that can be assigned to distinct tasks.

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“…Because these also interact with nuclear components, including A-type lamins (24,25,28), and a histone acetyl transferase [in the case of Sun1 (29)], Sun-nesprin pairs represent links in a molecular chain connecting the cytoskeleton to nuclear structures. We refer to these as LINC complexes (linker of the cytoskeleton and nucleoskeleton).…”

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confidence: 99%

Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization

Roux

Crisp

Liu

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Nucleocytoplasmic coupling is mediated by outer nuclear membrane (ONM) nesprin proteins and inner nuclear membrane Sun proteins. Interactions spanning the perinuclear space create nesprin-Sun complexes connecting the cytoskeleton to nuclear components. A search for proteins displaying a conserved C-terminal sequence present in nesprins 1-3 identified nesprin 4 (Nesp4), a new member of this family. Nesp4 is a kinesin-1-binding protein that displays Sun-dependent localization to the ONM. Expression of Nesp4 is associated with dramatic changes in cellular organization involving relocation of the centrosome and Golgi apparatus relative to the nucleus. These effects can be accounted for entirely by Nesp4's kinesin-binding function. The implication is that Nesp4 may contribute to microtubule-dependent nuclear positioning.centrosome ͉ LINC complex ͉ nuclear envelope T he nuclear envelope (NE) forms the interface between the nucleus and cytoplasm acting as a selective barrier that regulates nucleo-cytoplasmic traffic (1). In addition to this partition function, accumulating evidence reveals an essential role for the NE as a determinant of higher-order nuclear and chromatin organization (2). More surprising are findings that the NE directly impacts cytoskeletal architecture and in this way may help define the mechanical properties of the cell as a whole (3). The molecular bases for these effects are now emerging, uniting aspects of cellular physiology from mechanotransduction to nuclear positioning during differentiation and development (4).The NE is assembled from several elements, the most prominent being inner nuclear membranes (INMs) and outer nuclear membranes (ONMs) separated by a Ϸ40-nm gap or perinuclear space (PNS). The INM and ONM are joined where they are spanned by nuclear pore complexes (NPCs), the mediators of trafficking across the NE. The ONM also displays connections to the peripheral endoplasmic reticulum (ER). Accordingly, the INM, ONM, and ER represent a single membrane system with the PNS forming an extension of the ER lumen.The final feature of the NE is the nuclear lamina, a protein meshwork composed primarily of A-and B-type lamins that lines the nuclear face of the INM (2). The lamina is required for NE integrity and provides chromatin-anchoring sites at the nuclear periphery. Remarkably, aberrant A-type lamin expression, which is linked to several human diseases (5), is associated with altered cytoskeletal mechanics (3). The mechanisms underlying this phenomenon represent an intriguing biological problem.At least 60 NE membrane proteins are known (6). Although most likely reside in the INM, several ONM proteins have been identified (7). These include members of the mammalian nesprin (or syne) family (8, 9), Klarsicht (10) and 12) in Drosophila melanogaster, Anc-1 (13), and 16) in Caenorhabditis elegans, and Kms2 in the fission yeast Schizosaccharomyces pombe (17). A property that each of these has in common is that they interact with cytoskeletal components. They are also united in possessing a...

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Histone Acetyltransferase hALP and Nuclear Membrane Protein hsSUN1 Function in De-condensation of Mitotic Chromosomes

Cited by 104 publications

References 60 publications

Requirement for Sun1 in the expression of meiotic reproductive genes and piRNA

Requirement for Sun1 in the expression of meiotic reproductive genes and piRNA

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration

Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization

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