Necdin, A Postmitotic Neuron-specific Growth Suppressor, Interacts with Viral Transforming Proteins and Cellular Transcription Factor E2F1

Taniura, Hideo; Taniguchi, Naoko; Hara, Mizuki; Yoshikawa, Kunio

doi:10.1074/jbc.273.2.720

Cited by 159 publications

(167 citation statements)

References 27 publications

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“…Necdin is a 47-kDa protein that functions as a cell-growth suppressor in a manner similar to that of the retinoblastoma tumor suppressor protein, Rb (27,28). In our study, IP showed a faint band (Ϸ47 kDa) that was subjected to N-terminal amino acid sequence analysis.…”

Section: Discussionmentioning

confidence: 99%

Intracellular IL-1α-binding proteins contribute to biological functions of endogenous IL-1α in systemic sclerosis fibroblasts

Kawaguchi

Nishimagi²,

Tochimoto³

et al. 2006

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

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The aberrant production of precursor IL-1␣ (pre-IL-1␣) in skin fibroblasts that are derived from systemic sclerosis (SSc) is associated with the induction of IL-6 and procollagen, which contributes to the fibrosis of SSc. However, little is understood about how intracellular pre-IL-1␣ regulates the expression of the other molecules in fibroblasts. We report here that pre-IL-1␣ can form a complex with IL-1␣-binding proteins that is translocated into the nuclei of fibroblasts. Immunoprecipitation that used anti-human IL-1␣ Ab and 35 S-labeled nuclear extracts of fibroblasts showed three specific bands (Ϸ31, 35, and 65 kDa). The 31-kDa molecule was identified as pre-IL-1␣, and the 35-and 65-kDa molecules might be pre-IL-1␣-binding proteins. A partial sequencing for the 10 aa from the N-terminals of the molecules showed 100% homology for HAX-1 (HS1-associated protein X-1) and IL-1 receptor type II (IL-1RII). Suppression of the genes of HAX-1 or IL-1RII induced the inhibitory effects of IL-1 signal transduction, including production of IL-6 and procollagen, by fibroblasts. In particular, pre-IL-1␣ was not translocated into the nucleus by an inhibition of HAX-1. These findings reveal that nuclear localization of pre-IL-1␣ depends on the binding to HAX-1 and that biological activities might be elicited by the binding to both HAX-1 and IL-1RII in SSc fibroblasts.IL-1 receptor type II ͉ HS1-associated protein X-1 ͉ fibrosis ͉ collagen ͉ IL-6

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Section: Discussionmentioning

confidence: 99%

Intracellular IL-1α-binding proteins contribute to biological functions of endogenous IL-1α in systemic sclerosis fibroblasts

Kawaguchi

Nishimagi²,

Tochimoto³

et al. 2006

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

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“…Although the repeats in NRAGE are unrelated to those found in DAMAGE, the overall similarity in structure between DAMAGE and NRAGE suggests that they have common functions. A second MAGE protein, Necdin, is expressed in post-mitotic neurons and prevents cell cycle progression by inhibiting the transcription factor E2F1 (50). Necdin also has anti-apoptotic effects mediated by its interaction with p53 (51).…”

Section: Discussionmentioning

confidence: 99%

“…The presence of a possible NLS combined with our observation that DAMAGE resides within nuclei and/or in a perinuclear compartment are consistent with this hypothesis. In addition, the precedent that other MAGE proteins interact with transcription factors (50,53,54) and regulate cell cycle progression and apoptosis (46 -48, 51, 55) suggests that DAMAGE may have similar functions.…”

Section: ␣-Dystrobrevin Interaction With Damage/mage-e1 7021mentioning

confidence: 99%

DAMAGE, a Novel α-Dystrobrevin-associated MAGE Protein in Dystrophin Complexes

Albrecht

Froehner

2004

Journal of Biological Chemistry

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Mice rendered null for ␣-dystrobrevin, a component of the dystrophin complex, have muscular dystrophy, despite the fact that the sarcolemma remains relatively intact (Grady, R. M., Grange, R. W., Lau, K. S., Maimone, M. M., Nichol, M. C., Stull, J. T., and Sanes, J. R. (1999) Nat. Cell Biol. 1, 215-220) Thus, ␣-dystrobrevin may serve a signaling function that is important for the maintenance of muscle integrity. We have identified a new dystrobrevin-associated protein, DAMAGE, that may play a signaling role in brain, muscle, and peripheral nerve. In humans, DAMAGE is encoded by an intronless gene located at chromosome Xq13.1, a locus that contains genes involved in mental retardation. DAM-AGE associates directly with ␣-dystrobrevin, as shown by yeast two-hybrid, and co-immunoprecipitates with the dystrobrevin-syntrophin complex from brain. This co-immunoprecipitation is dependent on the presence of ␣-dystrobrevin but not ␤-dystrobrevin. The DAMAGE protein contains a potential nuclear localization signal, 30 12-amino acid repeats, and two MAGE homology domains. The domain structure of DAMAGE is similar to that of NRAGE, a MAGE protein that mediates p75 neurotrophin receptor signaling and neuronal apoptosis (Salehi, A. H., Roux, P. P., Kubu, C. J., Zeindler, C., Bhakar, A., Tannis, L. L., Verdi, J. M., and Barker, P. A. (2000) Neuron 27, 279 -288). DAMAGE is highly expressed in brain and is present in the cell bodies and dendrites of hippocampal and Purkinje neurons. In skeletal muscle, DAMAGE is at the postsynaptic membrane and is associated with a subset of myonuclei. DAMAGE is also expressed in peripheral nerve, where it localizes along with other members of the dystrophin complex to the perineurium and myelin. These results expand the role of dystrobrevin and the dystrophin complex in membrane signaling and disease.The dystrophin glycoprotein complex links the actin cytoskeleton to the extracellular matrix in skeletal muscle. In addition, recent studies (1-7) have shown that the dystrophin complex is critical for the localization of a variety of signaling molecules to the skeletal muscle sarcolemma. Thus, the dystrophin complex functions as both a structural link to the extracellular matrix and as a scaffold that concentrates and stabilizes functionally inter-related signaling proteins at the muscle cell membrane.Part of the signaling function of the dystrophin complex may be mediated by the dystrobrevins. The role of the dystrobrevins in signaling is not fully understood; however, targeted disruption of the ␣-dystrobrevin gene in mice results in muscle pathology without the membrane fragility characteristic of dystrophin-deficient muscular dystrophy (8). These findings suggest that ␣-dystrobrevin is important for muscle function but in a non-structural way. Dystrobrevin has no enzymatic activity of its own; therefore, the involvement of dystrobrevin in signaling pathways is dependent on its interaction with other proteins.The dystrobrevins are transcribed from two separate genes, designated ␣ and ␤, that shar...

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“…Interestingly, NRAGE shows a high homology in its carboxyl-terminal with the melanoma associated antigen (MAGE) family, which codes for antigens that present on many human tumors, although their intracellular function is mostly unknown. One exception is necdin, a postmitotic neuron-specific growth suppressor that can interact with both intracellular proteins such as E2F1 and p53 and viral transforming proteins such as adenovirus E1A (16).…”

mentioning

confidence: 99%

Neurotrophin Receptor-interacting Mage Homologue Is an Inducible Inhibitor of Apoptosis Protein-interacting Protein That Augments Cell Death

Jordan

Dinev

LeMellay

et al. 2001

Journal of Biological Chemistry

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The inhibitor of apoptosis proteins (IAPs) have been shown to interact with a growing number of intracellular proteins and pathways to fulfil their anti-apoptotic role. In the search for novel IAP-interacting proteins we identified the neurotrophin receptor-interacting MAGE homologue (NRAGE) as being able to bind to the avian IAP homologue ITA. This interaction requires the RING domain of ITA. NRAGE additionally coimmunoprecipitates with XIAP. When overexpressed in 32D cells NRAGE augments interleukin-3 withdrawal induced apoptosis, possibly through binding endogenous XIAP. Moreover, NRAGE is able to overcome the anti-apoptotic effect of Bcl-2.

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Necdin, A Postmitotic Neuron-specific Growth Suppressor, Interacts with Viral Transforming Proteins and Cellular Transcription Factor E2F1

Cited by 159 publications

References 27 publications

Intracellular IL-1α-binding proteins contribute to biological functions of endogenous IL-1α in systemic sclerosis fibroblasts

Intracellular IL-1α-binding proteins contribute to biological functions of endogenous IL-1α in systemic sclerosis fibroblasts

DAMAGE, a Novel α-Dystrobrevin-associated MAGE Protein in Dystrophin Complexes

Neurotrophin Receptor-interacting Mage Homologue Is an Inducible Inhibitor of Apoptosis Protein-interacting Protein That Augments Cell Death

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