The physical interactions between p37env-mos and tubulin structures

Wenlong Bai, Balraj Singh, Yandan Yang, Louis S. Ramagli, Michael Nash, Norbert K. Herzog, Ralph B. Arlinghaus

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The c-mos protein has been reported to be complexed with tubulin and to co-localize with microtubules in unfertilized Xenopus eggs as well as in NIH3T3 cells transformed by the Xenopus c-mos gene. We performed experiments to determine whether the viral mos protein, p37v-mos, also associates with tubulin. Both mouse c-mos and v-mos proteins synthesized in vitro co-polymerized with tubulin. Upon incubation at 37°C, essentially all of the mos protein (both viral and cellular) co-polymerized with tubulin, while more than 50% of the tubulin remained in the depolymerized state. The mos-tubulin interaction was specific, as indicated by the insolubility of the v-mos protein following a second cycle of temperature-dependent depolymerization/polymerization. Beta-tubulin was shown to co-precipitate with p3Tv-mos and to be phosphorylated by the mos kinase in vitro. Although both v-mos and c-mos proteins co-polymerize with tubulin, p37v-mos behaved differently from p39c-mos on gel filtration columns under conditions that favor disassembly of microtubules. Like Xenopus c-mos, the bulk of the mouse c-mos protein synthesized in vitro appeared in structures that fractionate at about 500 kDa. In contrast to c-mos, the majority of the v-mos protein, either isolated from stably transformed NIH3T3 cells or synthesized in vitro, eluted in the 100 kDa fraction, cofractionating with tubulin dimers. Therefore, the v-mos protein appears to have a higher affinity for unpolymerized tubulin than c-mos, under conditions that favor disassembly of microtubules.

Original languageEnglish (US)
Pages (from-to)493-500
Number of pages8
JournalOncogene
Volume7
Issue number3
StatePublished - Mar 1992
Externally publishedYes

Fingerprint

Tubulin
Oncogene Proteins v-mos
Proto-Oncogene Proteins c-mos
Xenopus
Microtubules
Viral Proteins
mos Genes
Polymerization
Gel Chromatography
Ovum
Phosphotransferases
Temperature
In Vitro Techniques

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

Cite this

Bai, W., Singh, B., Yang, Y., Ramagli, L. S., Nash, M., Herzog, N. K., & Arlinghaus, R. B. (1992). The physical interactions between p37env-mos and tubulin structures. Oncogene, 7(3), 493-500.

The physical interactions between p37env-mos and tubulin structures. / Bai, Wenlong; Singh, Balraj; Yang, Yandan; Ramagli, Louis S.; Nash, Michael; Herzog, Norbert K.; Arlinghaus, Ralph B.

In: Oncogene, Vol. 7, No. 3, 03.1992, p. 493-500.

Research output: Contribution to journalArticle

Bai, W, Singh, B, Yang, Y, Ramagli, LS, Nash, M, Herzog, NK & Arlinghaus, RB 1992, 'The physical interactions between p37env-mos and tubulin structures', Oncogene, vol. 7, no. 3, pp. 493-500.
Bai W, Singh B, Yang Y, Ramagli LS, Nash M, Herzog NK et al. The physical interactions between p37env-mos and tubulin structures. Oncogene. 1992 Mar;7(3):493-500.
Bai, Wenlong ; Singh, Balraj ; Yang, Yandan ; Ramagli, Louis S. ; Nash, Michael ; Herzog, Norbert K. ; Arlinghaus, Ralph B. / The physical interactions between p37env-mos and tubulin structures. In: Oncogene. 1992 ; Vol. 7, No. 3. pp. 493-500.
@article{704bd4978ac241e29f058ac37d21d168,
title = "The physical interactions between p37env-mos and tubulin structures",
abstract = "The c-mos protein has been reported to be complexed with tubulin and to co-localize with microtubules in unfertilized Xenopus eggs as well as in NIH3T3 cells transformed by the Xenopus c-mos gene. We performed experiments to determine whether the viral mos protein, p37v-mos, also associates with tubulin. Both mouse c-mos and v-mos proteins synthesized in vitro co-polymerized with tubulin. Upon incubation at 37°C, essentially all of the mos protein (both viral and cellular) co-polymerized with tubulin, while more than 50{\%} of the tubulin remained in the depolymerized state. The mos-tubulin interaction was specific, as indicated by the insolubility of the v-mos protein following a second cycle of temperature-dependent depolymerization/polymerization. Beta-tubulin was shown to co-precipitate with p3Tv-mos and to be phosphorylated by the mos kinase in vitro. Although both v-mos and c-mos proteins co-polymerize with tubulin, p37v-mos behaved differently from p39c-mos on gel filtration columns under conditions that favor disassembly of microtubules. Like Xenopus c-mos, the bulk of the mouse c-mos protein synthesized in vitro appeared in structures that fractionate at about 500 kDa. In contrast to c-mos, the majority of the v-mos protein, either isolated from stably transformed NIH3T3 cells or synthesized in vitro, eluted in the 100 kDa fraction, cofractionating with tubulin dimers. Therefore, the v-mos protein appears to have a higher affinity for unpolymerized tubulin than c-mos, under conditions that favor disassembly of microtubules.",
author = "Wenlong Bai and Balraj Singh and Yandan Yang and Ramagli, {Louis S.} and Michael Nash and Herzog, {Norbert K.} and Arlinghaus, {Ralph B.}",
year = "1992",
month = "3",
language = "English (US)",
volume = "7",
pages = "493--500",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "3",

}

TY - JOUR

T1 - The physical interactions between p37env-mos and tubulin structures

AU - Bai, Wenlong

AU - Singh, Balraj

AU - Yang, Yandan

AU - Ramagli, Louis S.

AU - Nash, Michael

AU - Herzog, Norbert K.

AU - Arlinghaus, Ralph B.

PY - 1992/3

Y1 - 1992/3

N2 - The c-mos protein has been reported to be complexed with tubulin and to co-localize with microtubules in unfertilized Xenopus eggs as well as in NIH3T3 cells transformed by the Xenopus c-mos gene. We performed experiments to determine whether the viral mos protein, p37v-mos, also associates with tubulin. Both mouse c-mos and v-mos proteins synthesized in vitro co-polymerized with tubulin. Upon incubation at 37°C, essentially all of the mos protein (both viral and cellular) co-polymerized with tubulin, while more than 50% of the tubulin remained in the depolymerized state. The mos-tubulin interaction was specific, as indicated by the insolubility of the v-mos protein following a second cycle of temperature-dependent depolymerization/polymerization. Beta-tubulin was shown to co-precipitate with p3Tv-mos and to be phosphorylated by the mos kinase in vitro. Although both v-mos and c-mos proteins co-polymerize with tubulin, p37v-mos behaved differently from p39c-mos on gel filtration columns under conditions that favor disassembly of microtubules. Like Xenopus c-mos, the bulk of the mouse c-mos protein synthesized in vitro appeared in structures that fractionate at about 500 kDa. In contrast to c-mos, the majority of the v-mos protein, either isolated from stably transformed NIH3T3 cells or synthesized in vitro, eluted in the 100 kDa fraction, cofractionating with tubulin dimers. Therefore, the v-mos protein appears to have a higher affinity for unpolymerized tubulin than c-mos, under conditions that favor disassembly of microtubules.

AB - The c-mos protein has been reported to be complexed with tubulin and to co-localize with microtubules in unfertilized Xenopus eggs as well as in NIH3T3 cells transformed by the Xenopus c-mos gene. We performed experiments to determine whether the viral mos protein, p37v-mos, also associates with tubulin. Both mouse c-mos and v-mos proteins synthesized in vitro co-polymerized with tubulin. Upon incubation at 37°C, essentially all of the mos protein (both viral and cellular) co-polymerized with tubulin, while more than 50% of the tubulin remained in the depolymerized state. The mos-tubulin interaction was specific, as indicated by the insolubility of the v-mos protein following a second cycle of temperature-dependent depolymerization/polymerization. Beta-tubulin was shown to co-precipitate with p3Tv-mos and to be phosphorylated by the mos kinase in vitro. Although both v-mos and c-mos proteins co-polymerize with tubulin, p37v-mos behaved differently from p39c-mos on gel filtration columns under conditions that favor disassembly of microtubules. Like Xenopus c-mos, the bulk of the mouse c-mos protein synthesized in vitro appeared in structures that fractionate at about 500 kDa. In contrast to c-mos, the majority of the v-mos protein, either isolated from stably transformed NIH3T3 cells or synthesized in vitro, eluted in the 100 kDa fraction, cofractionating with tubulin dimers. Therefore, the v-mos protein appears to have a higher affinity for unpolymerized tubulin than c-mos, under conditions that favor disassembly of microtubules.

UR - http://www.scopus.com/inward/record.url?scp=0026610961&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026610961&partnerID=8YFLogxK

M3 - Article

C2 - 1532247

AN - SCOPUS:0026610961

VL - 7

SP - 493

EP - 500

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 3

ER -