The Prader–Willi syndrome protein necdin interacts with the E1A-like inhibitor of differentiation EID-1 and promotes myoblast differentiation

Bush, Jason; Wevrick, Rachel

doi:10.1111/j.1432-0436.2008.00281.x

Cited by 29 publications

(41 citation statements)

References 53 publications

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“…Perhaps binding to MAGE/Nse3-like proteins shields EID1 from FBXO21 during the cell cycle. The ability of the MAGE-related protein Necdin to bind to and stabilize EID1 is consistent with this idea (16). Similarly, the EID1 degron overlaps with the EID1 pRB-binding region, suggesting that EID1 stability could also be influenced by pRB and providing a mechanistic explanation for the induction of EID1 in cells observed after exogenous pRB expression (5).…”

Section: Discussionsupporting

confidence: 65%

“…EID1 also binds to small heterodimer partner (SHP) [also called NR0B2 (nuclear receptor subfamily 0, group B, member 2)], which is a transcriptional corepressor for various steroid hormone family transcription factors (11)(12)(13)(14). In cell-based models, overexpression of EID1 likewise represses transcription factors and blocks differentiation (5,6,11,(14)(15)(16)(17). These cellular activities correlate with its ability to inhibit p300 histone acetyltransferase in vitro and in vivo (5,6,11).…”

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confidence: 99%

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Peptidic degron in EID1 is recognized by an SCF E3 ligase complex containing the orphan F-box protein FBXO21

Zhang

Adelmant

et al. 2015

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

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EP300-interacting inhibitor of differentiation 1 (EID1) belongs to a protein family implicated in the control of transcription, differentiation, DNA repair, and chromosomal maintenance. EID1 has a very short half-life, especially in G0 cells. We discovered that EID1 contains a peptidic, modular degron that is necessary and sufficient for its polyubiquitylation and proteasomal degradation. We found that this degron is recognized by an Skp1, Cullin, and F-box (SCF)-containing ubiquitin ligase complex that uses the F-box Only Protein 21 (FBXO21) as its substrate recognition subunit. SCF FBXO21 polyubiquitylates EID1 both in vitro and in vivo and is required for the efficient degradation of EID1 in both cycling and quiescent cells. The EID1 degron partially overlaps with its retinoblastoma tumor suppressor protein-binding domain and is congruent with a previously defined melanomaassociated antigen-binding motif shared by EID family members, suggesting that binding to retinoblastoma tumor suppressor and melanoma-associated antigen family proteins could affect the polyubiquitylation and turnover of EID family members in cells.degradation | ubiquitylation | cell cycle | G0 | pRB

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Section: Discussionsupporting

confidence: 65%

mentioning

confidence: 99%

Peptidic degron in EID1 is recognized by an SCF E3 ligase complex containing the orphan F-box protein FBXO21

Zhang

Adelmant

et al. 2015

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

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“…Neurons from mice lacking necdin display reduced differentiation and increased apoptosis (Aebischer, 2011;Andrieu et al, 2003;Kurita et al, 2006;Kuwako et al, 2005;Pagliardini et al, 2005;Tennese et al, 2008). The capacity for differentiation of mesenchymal progenitor cells into muscle is reduced in these mice, as is the regeneration capacity of muscle in post-natal mice (Bush and Wevrick, 2008;Deponti et al, 2007). Loss of a second MAGE protein, Maged1, impairs myoblast differentiation in mice (Nguyen et al, 2010).…”

Section: Introductionmentioning

confidence: 96%

Loss of the Prader–Willi obesity syndrome protein necdin promotes adipogenesis

Bush

Wevrick

2012

Gene

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“…The genetic inactivation of the Necdin gene is associated with a developmental disorder in humans, Prader-Willi syndrome (PWS), in which three other genes are inactivated (11,18). The main features which characterize this syndrome are a delay in development; short stature; abnormalities in behavior; the onset of severe obesity in childhood; a consistent drive to eat, referred to as hyperphagia; inadequate ventilation; and reproductive system defects (11,18).…”

mentioning

confidence: 99%

“…The main features which characterize this syndrome are a delay in development; short stature; abnormalities in behavior; the onset of severe obesity in childhood; a consistent drive to eat, referred to as hyperphagia; inadequate ventilation; and reproductive system defects (11,18). Necdin belongs to a family of proteins called the MAGE proteins, which are increasingly shown to have roles in a number of cellular processes, including cell cycle regulation and cell death (5).…”

mentioning

confidence: 99%

EBNA3C Can Modulate the Activities of the Transcription Factor Necdin in Association with Metastasis Suppressor Protein Nm23-H1

Kaul

Murakami

Lan

et al. 2009

J Virol

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Previous studies have demonstrated the interaction between the Epstein-Barr virus (EBV) nuclear antigen 3C (EBNA3C) and the metastatic suppressorEpstein-Barr virus (EBV) is a human gammaherpesvirus which predominantly targets B cells and epithelial cells and is associated with a number of human cancers, including Burkitt's lymphoma, nasopharyngeal carcinoma, Hodgkin's disease, AIDS-associated and transplant-associated immunoblastic lymphoma, and, controversially, invasive breast carcinoma (9, 61). In vitro infection of B cells with EBV gives rise to lymphoblastoid cell lines (LCLs) which express a subset of 12 latent viral transcripts (61). These 12 transcripts encode six nuclear antigens (EBNAs), three latent membrane proteins, two early RNAs (32), and the BARF transcripts (61). Studies have shown that EBNA3C, one of the six nuclear antigens, interacts with the suppressor of cell migration and metastasis Nm23-H1 (69). This interaction between Nm23-H1 and EBNA3C has been shown to result in an increase in transcriptional activity on a targeted responsive promoter (70). Nm23-H1 tethered to DNA by a Gal4 DNA binding domain can activate transcription from a basal promoter at relatively low levels. However, when EBNA3C was introduced, the transactivation activity was shown to be substantially increased (70). These results suggest that Nm23-H1 may possess transcriptional regulatory activities which could function independent of its direct binding with DNA. This could possibly be through its interaction with EBNA3C (69). Interestingly, the presence of EBNA3C mediates the cellular translocation of Nm23-H1 from a mostly cytoplasmic to a predominantly nuclear signal. Moreover, EBNA3C can reverse the antimigratory effects of Nm23-H1 in vitro (69) as well as in vivo (23). The interaction between EBNA3C and Nm23-H1 has also been shown to be important in the regulation of COX-2, MMP-9, and alpha V integrin (13,24,26).The Nm23 gene family is highly conserved among a wide variety of eukaryotic species. Eight Nm23 genes have been identified for humans: Nm23-H1 (62), Nm23-H2 (68), Nm23-H3 (79), Nm23-H4 (45), Nm23-H5 (47), 76),. Members of the Nm23 gene family are structurally and functionally conserved, consisting of four to six identically folded subunits enclosing a large (25-Å) central cavity (84). Expression of Nm23 genes has been linked to suppression of tumor metastasis, differentiation, apoptosis, proliferation, and DNA mutation rate (14) and is also associated with nucleoside diphosphate (NDP) kinase activity (7,49,82), serine phosphorylation (8,20,37,48), histidine protein kinase activities (81), and transcriptional stimulatory activities (2,6,59,60). The human Nm23-H1 gene product is the best-characterized member of this family of proteins. It is 152 amino acids (aa) in length with leucine repeats and alpha-helical and basic domains (61). Nm23-H1 is 88% identical to Nm23-H2 and maps 4 kb apart at position q21.3 on

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The Prader–Willi syndrome protein necdin interacts with the E1A-like inhibitor of differentiation EID-1 and promotes myoblast differentiation

Cited by 29 publications

References 53 publications

Peptidic degron in EID1 is recognized by an SCF E3 ligase complex containing the orphan F-box protein FBXO21

Peptidic degron in EID1 is recognized by an SCF E3 ligase complex containing the orphan F-box protein FBXO21

Loss of the Prader–Willi obesity syndrome protein necdin promotes adipogenesis

EBNA3C Can Modulate the Activities of the Transcription Factor Necdin in Association with Metastasis Suppressor Protein Nm23-H1

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