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anti-Human SUN2 Anticorps:
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Mouse (Murine) Monoclonal SUN2 Primary Antibody pour ICC, IF - ABIN1042682
Haque, Mazzeo, Patel, Smallwood, Ellis, Shanahan, Shackleton: Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. dans The Journal of biological chemistry 2010
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Human Monoclonal SUN2 Primary Antibody pour ICC, IF - ABIN1042681
Hodzic, Yeater, Bengtsson, Otto, Stahl: Sun2 is a novel mammalian inner nuclear membrane protein. dans The Journal of biological chemistry 2004
While Sun1 and Sun2 in HeLa cells are each able to bind KASH-domains, Sun1 is more efficiently incorporated into LINC complexes under normal growth conditions. Furthermore, the balance of Sun1 and Sun2 incorporated into LINC complexes is cell type-specific and is correlated with SRF/Mkl1-dependent gene expression.
Thus, AID is a conserved functional domain in SUN proteins and this work provides the structural evidence to support the conversation of the AID-mediated autoinhibition of SUN proteins.
SUN1/SUN2 may function redundantly in early HIV-1 infection steps and therefore influence HIV-1 replication and pathogenesis.
These results demonstrate that SUN2 is required for the optimal activation and proliferation of primary CD4 T cells and suggest that the disruption of these processes explains the contribution of endogenous SUN2 to HIV infection in primary lymphocytes and show that CypA is not required for the decreased infection observed in SUN2-silenced cells.
SUN2 exerts tumor suppressor functions by suppressing the Warburg effect in lung cancer
SUN2 overexpression perturbs both nuclear shape and early events of HIV infection
Nuclear envelope associated endosome-mediated transfer depends on the nuclear envelope proteins SUN1 and SUN2, as well as the Sec61 translocon complex.
An important role for SUN1 and SUN2 in muscle disease pathogenesis.
SUN2 as a tumor suppressor mediates miR-221 and miR-222 functions in central nervous system embryonal tumors.
Codepletion of SUN1/2 slows cell proliferation and results in an accumulation of morphologically defective and disoriented mitotic spindles.
Study presents crystal structures of the human SUN2-KASH1/2 complex, i.e. SUN2 complexed with the C-terminal 29 residues of human Nesprin-1 or -2 (the core of the LINC complex).
the crystal structure of the SUN2 protein SUN domain
Data found that expression of lamin A but not lamin C partly restored the nuclear envelope localization of SUN2.
Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development
Data suggest that SUN2 represents the first mammalian inner nuclear membrane (INM) protein relying on a functional nuclear localization signal, a Golgi retrieval signal and a perinuclear domain to mediate targeting to the INM.
perturbations in lamin A-SUN1 and SUN2 protein interactions may underlie the opposing effects of EDMD and HGPS mutations on nuclear and cellular mechanics
SUN1 and SUN2 may form a physical interaction between the nuclear envelope and the centrosome
our results clearly indicate that SUN1 and SUN2, at least partially, fulfill redundant meiotic functions
Sun2 has a role in DNA damage response.
Syne-2, SUN1 and SUN2 play critical roles during interkinetic nuclear migration and photoreceptor cell migration in the mouse retina development.
Sun2 is part of a membrane-spanning fibrillar complex that interconnects attached telomeres with cytoplasmic structures
These results clearly indicate that SUN1 and SUN2 function critically in skeletal muscle cells for Syne-1 localization at the nuclear envelope, which is essential for proper myonuclear positioning.
indicate that the SUN2-KASH complexes mediate the coupling between the nucleus and the centrosome and provide anchors in the nuclear envelope for cytoplasmic dynein/dynactin during neuronal migration.
SUN1 (MIM 607723) and SUN2 are inner nuclear membrane (INM) proteins that play a major role in nuclear-cytoplasmic connection by formation of a 'bridge' across the nuclear envelope, known as the LINC complex, via interaction with the conserved luminal KASH domain of nesprins (e.g., SYNE1\; MIM 608441) located in the outer nuclear membrane (ONM). The LINC complex provides a direct connection between the nuclear lamina and the cytoskeleton, which contributes to nuclear positioning and cellular rigidity (summary by Haque et al., 2010
SUN domain-containing protein 2
, Sad1 unc-84 domain protein 2
, nuclear envelope protein
, protein unc-84 homolog B
, rab5-interacting protein
, sad1/unc-84 protein-like 2
, unc-84 homolog B