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Gas2, a growth arrest-specific protein, is a component of the microfilament network system

In this report we analyze the protein product of a growth arrest- specific gene, gas2, by means of an affinity-purified antibody raised against the protein produced in bacteria. The regulation of Gas2 biosynthesis reflects the pattern of mRNA expression (Schneider, C., R. King, and L. Philipson. 198...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1992
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289493/
https://www.ncbi.nlm.nih.gov/pubmed/1607387
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description In this report we analyze the protein product of a growth arrest- specific gene, gas2, by means of an affinity-purified antibody raised against the protein produced in bacteria. The regulation of Gas2 biosynthesis reflects the pattern of mRNA expression (Schneider, C., R. King, and L. Philipson. 1988. Cell. 54:787-793): its relative level is tightly associated with growth arrest. Gas2 seems to be regulated also at the posttranslational level via a phosphorylation mechanism. Gas2 is well conserved during the evolution with the same apparent molecular mass (36 kD) between mouse and human. We also demonstrate that Gas2 is a component of the microfilament system. It colocalizes with actin fiber, at the cell border and also along the stress fiber, in growth- arrested NIH 3T3 cells. The pattern of distribution, detected in arrested cells, can also be observed in growing cells when they are microinjected with the purified GST-Gas2 protein. In none of the analyzed oncogene-transformed NIH 3T3 cell lines was Gas2 expression induced under serum starvation.
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spelling pubmed-22894932008-05-01 Gas2, a growth arrest-specific protein, is a component of the microfilament network system J Cell Biol Articles In this report we analyze the protein product of a growth arrest- specific gene, gas2, by means of an affinity-purified antibody raised against the protein produced in bacteria. The regulation of Gas2 biosynthesis reflects the pattern of mRNA expression (Schneider, C., R. King, and L. Philipson. 1988. Cell. 54:787-793): its relative level is tightly associated with growth arrest. Gas2 seems to be regulated also at the posttranslational level via a phosphorylation mechanism. Gas2 is well conserved during the evolution with the same apparent molecular mass (36 kD) between mouse and human. We also demonstrate that Gas2 is a component of the microfilament system. It colocalizes with actin fiber, at the cell border and also along the stress fiber, in growth- arrested NIH 3T3 cells. The pattern of distribution, detected in arrested cells, can also be observed in growing cells when they are microinjected with the purified GST-Gas2 protein. In none of the analyzed oncogene-transformed NIH 3T3 cell lines was Gas2 expression induced under serum starvation. The Rockefeller University Press 1992-06-02 /pmc/articles/PMC2289493/ /pubmed/1607387 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Gas2, a growth arrest-specific protein, is a component of the microfilament network system
title Gas2, a growth arrest-specific protein, is a component of the microfilament network system
title_full Gas2, a growth arrest-specific protein, is a component of the microfilament network system
title_fullStr Gas2, a growth arrest-specific protein, is a component of the microfilament network system
title_full_unstemmed Gas2, a growth arrest-specific protein, is a component of the microfilament network system
title_short Gas2, a growth arrest-specific protein, is a component of the microfilament network system
title_sort gas2, a growth arrest-specific protein, is a component of the microfilament network system
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289493/
https://www.ncbi.nlm.nih.gov/pubmed/1607387