MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon

C. J. Liu, H. Wang, Z. Zhao, S. Yu, Y. B. Lu, J. Meyer, G. Chatterjee, S. Deschamps, B. A. Roe, P. Lengyel

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

p204, an interferon-inducible p200 family protein, inhibits rRNA synthesis in fibroblasts by blocking the binding of the upstream binding factor transcription factor to DNA. Here we report that among 10 adult mouse tissues tested, the level of p204 was highest in heart and skeletal muscles. In cultured C2C12 skeletal muscle myoblasts, p204 was nucleoplasmic and its level was low. During myoblast fusion this level strongly increased, p204 became phosphorylated, and the bulk of p204 appeared in the cytoplasm of the myotubes. Leptomycin B, an inhibitor of nuclear export that blocked myoblast fusion, inhibited the nuclear export signal-dependent translocation of p204 to the cytoplasm. The increase in the p204 level during myablast fusion was a consequence of MyoD transcription factor binding to several MyaD-specific sequences in the gene encoding p204, followed by transcription. Overexpression of p204 (in C2C12 myoblasts carrying an inducible p204 expression plasmid) accelerated the fusion of myoblasts to myotubes in differentiation medium and induced the fusion even in growth medium. The level of p204 in mouse heart muscle strongly increased during differentiation; it was barely detectable in 10.5-day-old embryos, reached the peak level in 16.5-day-old embryos, and remained high thereafter, p204 is the second p200 family protein (after p202a) found to be involved in muscle differentiation. (p202a was formerly designated p202. The new designation is due to the identification of a highly similar protein - p202b [H. Wang, G. Chatterjee, J. J. Meyer, C. J. Liu, N. A. Manjunath, P. Bray-Ward, and P. Lengyel, Genomics 60:281-294, 1999].) These results reveal that p204 and p202a function in both muscle differentiation and interferon action.

Original languageEnglish (US)
Pages (from-to)7024-7036
Number of pages13
JournalMolecular and Cellular Biology
Volume20
Issue number18
DOIs
StatePublished - Sep 28 2000

Fingerprint

Myoblasts
Interferons
Skeletal Muscle Fibers
Myocardium
Cytoplasm
Skeletal Muscle
Proteins
MyoD Protein
Transcription Factors
Embryonic Structures
Nuclear Export Signals
Skeletal Myoblasts
Muscles
Cell Nucleus Active Transport
Genomics
Plasmids
Fibroblasts
DNA
Growth
Genes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon. / Liu, C. J.; Wang, H.; Zhao, Z.; Yu, S.; Lu, Y. B.; Meyer, J.; Chatterjee, G.; Deschamps, S.; Roe, B. A.; Lengyel, P.

In: Molecular and Cellular Biology, Vol. 20, No. 18, 28.09.2000, p. 7024-7036.

Research output: Contribution to journalArticle

Liu, CJ, Wang, H, Zhao, Z, Yu, S, Lu, YB, Meyer, J, Chatterjee, G, Deschamps, S, Roe, BA & Lengyel, P 2000, 'MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon', Molecular and Cellular Biology, vol. 20, no. 18, pp. 7024-7036. https://doi.org/10.1128/MCB.20.18.7024-7036.2000
Liu, C. J. ; Wang, H. ; Zhao, Z. ; Yu, S. ; Lu, Y. B. ; Meyer, J. ; Chatterjee, G. ; Deschamps, S. ; Roe, B. A. ; Lengyel, P. / MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon. In: Molecular and Cellular Biology. 2000 ; Vol. 20, No. 18. pp. 7024-7036.
@article{6cb44538e33b4e04a0004672f7e62812,
title = "MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon",
abstract = "p204, an interferon-inducible p200 family protein, inhibits rRNA synthesis in fibroblasts by blocking the binding of the upstream binding factor transcription factor to DNA. Here we report that among 10 adult mouse tissues tested, the level of p204 was highest in heart and skeletal muscles. In cultured C2C12 skeletal muscle myoblasts, p204 was nucleoplasmic and its level was low. During myoblast fusion this level strongly increased, p204 became phosphorylated, and the bulk of p204 appeared in the cytoplasm of the myotubes. Leptomycin B, an inhibitor of nuclear export that blocked myoblast fusion, inhibited the nuclear export signal-dependent translocation of p204 to the cytoplasm. The increase in the p204 level during myablast fusion was a consequence of MyoD transcription factor binding to several MyaD-specific sequences in the gene encoding p204, followed by transcription. Overexpression of p204 (in C2C12 myoblasts carrying an inducible p204 expression plasmid) accelerated the fusion of myoblasts to myotubes in differentiation medium and induced the fusion even in growth medium. The level of p204 in mouse heart muscle strongly increased during differentiation; it was barely detectable in 10.5-day-old embryos, reached the peak level in 16.5-day-old embryos, and remained high thereafter, p204 is the second p200 family protein (after p202a) found to be involved in muscle differentiation. (p202a was formerly designated p202. The new designation is due to the identification of a highly similar protein - p202b [H. Wang, G. Chatterjee, J. J. Meyer, C. J. Liu, N. A. Manjunath, P. Bray-Ward, and P. Lengyel, Genomics 60:281-294, 1999].) These results reveal that p204 and p202a function in both muscle differentiation and interferon action.",
author = "Liu, {C. J.} and H. Wang and Z. Zhao and S. Yu and Lu, {Y. B.} and J. Meyer and G. Chatterjee and S. Deschamps and Roe, {B. A.} and P. Lengyel",
year = "2000",
month = "9",
day = "28",
doi = "10.1128/MCB.20.18.7024-7036.2000",
language = "English (US)",
volume = "20",
pages = "7024--7036",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "18",

}

TY - JOUR

T1 - MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon

AU - Liu, C. J.

AU - Wang, H.

AU - Zhao, Z.

AU - Yu, S.

AU - Lu, Y. B.

AU - Meyer, J.

AU - Chatterjee, G.

AU - Deschamps, S.

AU - Roe, B. A.

AU - Lengyel, P.

PY - 2000/9/28

Y1 - 2000/9/28

N2 - p204, an interferon-inducible p200 family protein, inhibits rRNA synthesis in fibroblasts by blocking the binding of the upstream binding factor transcription factor to DNA. Here we report that among 10 adult mouse tissues tested, the level of p204 was highest in heart and skeletal muscles. In cultured C2C12 skeletal muscle myoblasts, p204 was nucleoplasmic and its level was low. During myoblast fusion this level strongly increased, p204 became phosphorylated, and the bulk of p204 appeared in the cytoplasm of the myotubes. Leptomycin B, an inhibitor of nuclear export that blocked myoblast fusion, inhibited the nuclear export signal-dependent translocation of p204 to the cytoplasm. The increase in the p204 level during myablast fusion was a consequence of MyoD transcription factor binding to several MyaD-specific sequences in the gene encoding p204, followed by transcription. Overexpression of p204 (in C2C12 myoblasts carrying an inducible p204 expression plasmid) accelerated the fusion of myoblasts to myotubes in differentiation medium and induced the fusion even in growth medium. The level of p204 in mouse heart muscle strongly increased during differentiation; it was barely detectable in 10.5-day-old embryos, reached the peak level in 16.5-day-old embryos, and remained high thereafter, p204 is the second p200 family protein (after p202a) found to be involved in muscle differentiation. (p202a was formerly designated p202. The new designation is due to the identification of a highly similar protein - p202b [H. Wang, G. Chatterjee, J. J. Meyer, C. J. Liu, N. A. Manjunath, P. Bray-Ward, and P. Lengyel, Genomics 60:281-294, 1999].) These results reveal that p204 and p202a function in both muscle differentiation and interferon action.

AB - p204, an interferon-inducible p200 family protein, inhibits rRNA synthesis in fibroblasts by blocking the binding of the upstream binding factor transcription factor to DNA. Here we report that among 10 adult mouse tissues tested, the level of p204 was highest in heart and skeletal muscles. In cultured C2C12 skeletal muscle myoblasts, p204 was nucleoplasmic and its level was low. During myoblast fusion this level strongly increased, p204 became phosphorylated, and the bulk of p204 appeared in the cytoplasm of the myotubes. Leptomycin B, an inhibitor of nuclear export that blocked myoblast fusion, inhibited the nuclear export signal-dependent translocation of p204 to the cytoplasm. The increase in the p204 level during myablast fusion was a consequence of MyoD transcription factor binding to several MyaD-specific sequences in the gene encoding p204, followed by transcription. Overexpression of p204 (in C2C12 myoblasts carrying an inducible p204 expression plasmid) accelerated the fusion of myoblasts to myotubes in differentiation medium and induced the fusion even in growth medium. The level of p204 in mouse heart muscle strongly increased during differentiation; it was barely detectable in 10.5-day-old embryos, reached the peak level in 16.5-day-old embryos, and remained high thereafter, p204 is the second p200 family protein (after p202a) found to be involved in muscle differentiation. (p202a was formerly designated p202. The new designation is due to the identification of a highly similar protein - p202b [H. Wang, G. Chatterjee, J. J. Meyer, C. J. Liu, N. A. Manjunath, P. Bray-Ward, and P. Lengyel, Genomics 60:281-294, 1999].) These results reveal that p204 and p202a function in both muscle differentiation and interferon action.

UR - http://www.scopus.com/inward/record.url?scp=0033811255&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033811255&partnerID=8YFLogxK

U2 - 10.1128/MCB.20.18.7024-7036.2000

DO - 10.1128/MCB.20.18.7024-7036.2000

M3 - Article

C2 - 10958697

AN - SCOPUS:0033811255

VL - 20

SP - 7024

EP - 7036

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 18

ER -