Myc-Nick: A Cytoplasmic Cleavage Product of Myc that Promotes α-Tubulin Acetylation and Cell Differentiation

Conacci‐Sorrell, Maralice; Ngouenet, Celine; Eisenman, Robert N.

doi:10.1016/j.cell.2010.06.037

Cited by 197 publications

(229 citation statements)

References 50 publications

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“…Although a previous report showed that the Myc protein level increases in the nucleus upon H. pylori infection in a mouse macrophage cell line (21), our finding is consistent with several other studies showing that Myc localizes in the cytoplasm in various cells including lymphoid and differentiated myeloid cells, fibroblasts, and HeLa cells (24)(25)(26)(27). It has not been known why Myc is localized in the cytoplasm in some cells but not in the others.…”

Section: Discussionsupporting

confidence: 82%

A role for c-Myc in regulating anti-mycobacterial responses

Yim

Pong

et al. 2011

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

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c-Myc (Myc) is a well known transcription factor that regulates many essential cellular processes; however, its role in modulating immunity is not known. Here, we showed different species of mycobacteria can induce Myc expression via ERK1/2 and JNK activation. Unexpectedly, the induced Myc is localized in the cytoplasm but not in the nucleus. This induced Myc expression is associated with the induction of TNF-α and IL-6 and with the suppression of intracellular mycobacterial growth. To delineate the underlying mechanisms, we demonstrated that Myc enhances IRAK1 degradation, leading to specific activations of ERK1/2 and p38 MAPK but not Akt, and reduces IκBα protein recovery upon degradation. Hence, our findings may provide insights into a potential role for Myc in regulating the antimicrobial responses.cytokine | macrophages

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Section: Discussionsupporting

confidence: 82%

A role for c-Myc in regulating anti-mycobacterial responses

Yim

Pong

et al. 2011

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

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“…The recent study indicated that stress can induce the production of an Myc-nick (short form of c-Myc), which promoted cell survival and autophagy. 33,34 Our data indeed showed that Myc-nick was easily detected when cells were cultured at dense condition (Supplementary Figure S3C). However, Myc-nick cannot bind to (Supplementary Figure S3B) and be degraded by REGγ (Supplementary Figure S3C).…”

Section: Resultsmentioning

confidence: 52%

Regulation of c-Myc protein stability by proteasome activator REGγ

Jiang

Pan

et al. 2014

Cell Death Differ

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-Myc is a key transcriptional factor that has a prominent role in cell growth, differentiation and tumor development. Its protein levels are tightly controlled by ubiquitin-proteasome pathway and frequently deregulated in various cancers. Here, we report that the 11S proteasomal activator REGγ is a novel regulator of c-Myc abundance in cells. We showed that overexpression of wild-type REGγ, but not inactive mutants including N151Y and G250S, significantly promoted the degradation of c-Myc. Depletion of REGγ markedly increased the protein stability of c-Myc. REGγ interacts with the C-terminal region of c-Myc and regulates c-Myc protein turnover. Functionally, REGγ negatively regulates c-Myc-mediated cell proliferation. Interestingly, depletion of the Drosophila Reg homolog (dReg) in developing wings induced the upregulation of Drosophila Myc, which contributes to cell death. Collectively, these results suggest that REGγ proteasome has a conserved role in the regulation of Myc abundance in both mammalian cells and Drosophila.

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“…14) and GCN5 (ref. 16). The lack of detectable K40 a-tubulin acetylation in aTAT1 À / À mice reported here indicates that these other enzymes are not able to rescue deficiency of aTAT1, and therefore probably do not acetylate a-tubulin directly in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…14), San 15 , GCN5 (ref. 16) and aTAT1 (refs 9,17,18). Of these, compelling evidence supports a role for aTAT1 as the major a-tubulin acetyltransferase in Tetrahymena and C. elegans 9,17 .…”

mentioning

confidence: 99%

αTAT1 is the major α-tubulin acetyltransferase in mice

et al. 2013

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Post-translational modification of tubulin serves as a powerful means for rapidly adjusting the functional diversity of microtubules. Acetylation of the e-amino group of K40 in a-tubulin is one such modification that is highly conserved in ciliated organisms. Recently, aTAT1, a Gcn5-related N-acetyltransferase, was identified as an a-tubulin acetyltransferase in Tetrahymena and C. elegans. Here we generate mice with a targeted deletion of Atat1 to determine its function in mammals. Remarkably, we observe a loss of detectable K40 a-tubulin acetylation in these mice across multiple tissues and in cellular structures such as cilia and axons where acetylation is normally enriched. Mice are viable and develop normally, however, the absence of Atat1 impacts upon sperm motility and male mouse fertility, and increases microtubule stability. Thus, aTAT1 has a conserved function as the major a-tubulin acetyltransferase in ciliated organisms and has an important role in regulating subcellular specialization of subsets of microtubules.

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Myc-Nick: A Cytoplasmic Cleavage Product of Myc that Promotes α-Tubulin Acetylation and Cell Differentiation

Cited by 197 publications

References 50 publications

A role for c-Myc in regulating anti-mycobacterial responses

A role for c-Myc in regulating anti-mycobacterial responses

Regulation of c-Myc protein stability by proteasome activator REGγ

αTAT1 is the major α-tubulin acetyltransferase in mice

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