v-mos protein produced by in vitro translation has protein kinase activity

Herzog, Norbert K.; Nash, M.; Ramagli, Louis S.; Arlinghaus, Ralph B.

doi:10.1128/jvi.64.6.3093-3096.1990

Cited by 9 publications

(5 citation statements)

References 27 publications

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“…Considering the sensitivity of detection in this type of experiment, we believe that more than 90% of 35 S-labeled p37 v-mos stayed in the hypophosphorylated form after the kinase reaction and was therefore inactive. In a similar experiment, we previously found that most of the v-Mos produced by in vitro translation in rabbit reticulocyte lysate was also inactive (26). Whether a large percentage of v-Mos is also inactive in vivo is a more difficult question.…”

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confidence: 71%

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Inhibition of v-Mos Kinase Activity by Protein Kinase A

Yang

Herrmann

Arlinghaus

et al. 1996

Molecular and Cellular Biology

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We investigated the effect of cyclic AMP-dependent protein kinase (PKA ) on v-Mos kinase activity. Increase in PKA activity in vivo brought about either by forskolin treatment or by overexpression of PKA catalytic subunit resulted in a significant inhibition of v-Mos kinase activity. The purified PKA catalytic subunit was able to phosphorylate recombinant p37v-mos in vitro, suggesting that the mechanism of in vivo inhibition of v-Mos kinase involves direct phosphorylation by PKA. Combined tryptic phosphopeptide two-dimensional mapping analysis and in vitro mutagenesis studies indicated that Ser-56 is the major in vivo phosphorylation site on v-Mos. In vivo phosphorylation at Ser-56 correlated with slower migration of the v-Mos protein during sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, even though Ser-56 was phosphorylated by PKA, this phosphorylation was not involved in the inhibition of v-Mos kinase. The alanine-for-serine substitution at residue 56 did not affect the ability of v-Mos to autophosphorylate in vitro or, more importantly, to activate MEK1 in transformed NIH 3T3 cells. We identified Ser-263 phosphorylation, the Ala-263 mutant of v-Mos was not inhibited by forskolin treatment. From our results, we propose that the known inhibitory role of PKA in the initiation of oocyte maturation in mice could be explained at least in part by its inhibition of Mos kinase.

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confidence: 71%

“…4B). Significantly, the more slowly migrating species of GST-Mos, which typically result from v-Mos autophosphorylation (26,32), were present in dramatically reduced amounts upon PKA c coincubation. In this experiment, contaminating reticulocyte lysate kinase(s) also caused some phosphorylation of GST-Mos (e.g., Fig.…”

Section: Inhibition Of V-mos Kinase By Pkamentioning

confidence: 95%

Inhibition of v-Mos Kinase Activity by Protein Kinase A

Yang

Herrmann

Arlinghaus

et al. 1996

Molecular and Cellular Biology

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“…In mammalian gonad tissues Mos appears to play an important role in maturation of male and female germinal cells [27–29]. However, various other somatic cell lineages and tissues express significant amounts of Mos products [30–32]. Accumulation of Mos during skeletal muscle development suggested a particular function(s) of Mos in this tissue [33].…”

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confidence: 99%

Overexpression of Mos^rat proto‐oncogene product enhances the positive autoregulatory loop of MyoD

et al. 1998

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The myogenic b-HLH transcription factor MyoD activates expression of muscle-specific genes and autoregulates positively its own expression. Various factors such as growth factors and oncogene products repress transcriptional activity of MyoD. The c-mos proto-oncogene product, Mos, is a serine/ threonine kinase that can activate myogenic differentiation by specific phosphorylation of MyoD which favors heterodimerization of MyoD and E12 proteins. Here we show that overexpression of Mos enhances the expression level of MyoD protein in myoblasts although phosphorylation of MyoD by Mos does not modify its stability but promotes transcriptional transactivation of the MyoD promoter linked to the luciferase reporter gene. Moreover, co-expression of MyoD with Mos wt but not with the kinase-inactive Mos KM greatly enhances expression of endogenous MyoD protein and the DNA binding activity of MyoD/E12 heterodimers in 10T1/2 cells. Our data suggest that Mos increases the ability of MyoD to transactivate both musclespecific genes and its own promoter and could therefore participate in the positive autoregulation loop of MyoD and muscle differentiation.z 1998 Federation of European Biochemical Societies.

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“…Prestained molecular mass markers are shown on the left. Exposure time, 10 h. mobility in sodium dodecyl sulfate (SDS)-polyacrylamide gels (10,14). The major v-mos band produced from antimos(37-55) immune complexes derived from chronically Mo-MuSV-infected NIH 3T3 cells corresponds to the hyperphosphorylated species (Fig.…”

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“…4. v-mos proteins were immunoprecipitated with anti-mos(37-55) antibodies, and the autophosphorylation reaction was caried out as described previously (10,29). Lanes 1 and 2, Mo-MuSV v-mos; lanes 3 and 4, MPSV v-mos; lanes 5 and 6, ts159 MPSV v-mos; lanes 7 and 8, no RNA.…”

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v-mos proteins encoded by myeloproliferative sarcoma virus and its ts159 mutant

Singh

Stocking

Walker

et al. 1992

J Virol

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The myeloproliferative sarcoma virus (MPSV) v-mos protein was predicted to be identical in size to p39c``Os because of an observed one-base deletion in the seventh codon of the env-mos open reading frame, which would allow translation to initiate at the methionine equivalent to codon 32 of the env-mos gene. On the basis of published results, p39c-mos is known to have greatly reduced in vitro protein kinase activity compared with p37cnv-mos encoded by Moloney murine sarcoma virus. Unexpectedly, the relative activity of the MPSV v-mos protein kinase was comparable to that of p37 nvmos. Consistent with this finding, the size of MPSV v-mos protein was found to be similar to the size of p37''vsfoS. Moreover, the pattern and sizes of phosphorylated bands produced by autophosphorylation of the MPSV v-mos protein were similar to those of p37nern's. These results were confirmed by in vitro transcription-translation of the MPSV v-mos gene. Resequencing portions of the MPSV mos gene failed to show the deletion within codon 7. Except for the codon 262 deletion, other mutations characteristic of MPSV and temperature-sensitive MPSV v-mos genes were confirmed. A glycineto-arginine mutation at residue 338 of the MPSV env-mos sequence, previously shown to cause thermosensitivity of the mutant virus (termed ts159) transforming function, yielded a v-mos protein that had significantly reduced protein kinase activity in vitro. These findings indicate that MPSV, like other Moloney murine sarcoma virus strains, also encodes a functional env-mos protein.

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v-mos protein produced by in vitro translation has protein kinase activity

Cited by 9 publications

References 27 publications

Inhibition of v-Mos Kinase Activity by Protein Kinase A

Inhibition of v-Mos Kinase Activity by Protein Kinase A

Overexpression of Mos^rat proto‐oncogene product enhances the positive autoregulatory loop of MyoD

v-mos proteins encoded by myeloproliferative sarcoma virus and its ts159 mutant

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v-mos protein produced by in vitro translation has protein kinase activity

Cited by 9 publications

References 27 publications

Inhibition of v-Mos Kinase Activity by Protein Kinase A

Inhibition of v-Mos Kinase Activity by Protein Kinase A

Overexpression of Mosrat proto‐oncogene product enhances the positive autoregulatory loop of MyoD

v-mos proteins encoded by myeloproliferative sarcoma virus and its ts159 mutant

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Overexpression of Mos^rat proto‐oncogene product enhances the positive autoregulatory loop of MyoD