CIQUIBIC   05472
CENTRO DE INVESTIGACIONES EN QUIMICA BIOLOGICA DE CORDOBA
Unidad Ejecutora - UE
artículos
Título:
N-Terminal c-Fos tyrosine phosphorylation regulates c-Fos/ER association
Autor/es:
MAXIMILIANO MOISES PORTAL; GABRIEL ORLANDO FERRERO; BEATRIZ LEONOR CAPUTTO
Revista:
ONCOGENE
Editorial:
Nature Publishing Group
Referencias:
Lugar: Londres; Año: 2007 p. 3551 - 3558
ISSN:
0950-9232
Resumen:
c-Fos dephosphorylated on tyrosine (c-Fos), a component
of the activator protein-1 (AP-1) family of transcription
factors, is expressed at very low levels in resting cells.
However, its expression is rapidly upregulated in cells
undergoing G0 to S phase transition leading to AP-1-
dependent gene transcription responses. In addition,
cytoplasmic c-Fos associates to the endoplasmic reticulum
(ER) membranes and activates phospholipid synthesis
during cell growth and differentiation. Herein, it is shown
that in T98G cells, c-Fos/ER association and consequently
phospholipid synthesis activation is regulated by
the phosphorylated state of c-Fos tyrosine (tyr) residues.
The small amount of c-Fos present in quiescent T98G cells
is tyr-phosphorylated and not ER-membrane bound. In
growing cells, it is dephosphorylated, associated to ER
membranes and promotes phospholipid synthesis activation.
Impairing tyr-dephosphorylation abrogates phospholipid
synthesis activation and reduces proliferation rates to
those of quiescent cells. Substitution of tyr residues 10, 30,
106 and 337 evidence tyr 10 and 30 as relevant for this
regulatory phenomenon. It is concluded that phosphorylation
of tyr residues 10 and 30 of c-Fos regulate the rate
of synthesis of phospholipids by regulating c-Fos/ER
association.
dependent gene transcription responses. In addition,
cytoplasmic c-Fos associates to the endoplasmic reticulum
(ER) membranes and activates phospholipid synthesis
during cell growth and differentiation. Herein, it is shown
that in T98G cells, c-Fos/ER association and consequently
phospholipid synthesis activation is regulated by
the phosphorylated state of c-Fos tyrosine (tyr) residues.
The small amount of c-Fos present in quiescent T98G cells
is tyr-phosphorylated and not ER-membrane bound. In
growing cells, it is dephosphorylated, associated to ER
membranes and promotes phospholipid synthesis activation.
Impairing tyr-dephosphorylation abrogates phospholipid
synthesis activation and reduces proliferation rates to
those of quiescent cells. Substitution of tyr residues 10, 30,
106 and 337 evidence tyr 10 and 30 as relevant for this
regulatory phenomenon. It is concluded that phosphorylation
of tyr residues 10 and 30 of c-Fos regulate the rate
of synthesis of phospholipids by regulating c-Fos/ER
association.
dependent gene transcription responses. In addition,
cytoplasmic c-Fos associates to the endoplasmic reticulum
(ER) membranes and activates phospholipid synthesis
during cell growth and differentiation. Herein, it is shown
that in T98G cells, c-Fos/ER association and consequently
phospholipid synthesis activation is regulated by
the phosphorylated state of c-Fos tyrosine (tyr) residues.
The small amount of c-Fos present in quiescent T98G cells
is tyr-phosphorylated and not ER-membrane bound. In
growing cells, it is dephosphorylated, associated to ER
membranes and promotes phospholipid synthesis activation.
Impairing tyr-dephosphorylation abrogates phospholipid
synthesis activation and reduces proliferation rates to
those of quiescent cells. Substitution of tyr residues 10, 30,
106 and 337 evidence tyr 10 and 30 as relevant for this
regulatory phenomenon. It is concluded that phosphorylation
of tyr residues 10 and 30 of c-Fos regulate the rate
of synthesis of phospholipids by regulating c-Fos/ER
association.
dependent gene transcription responses. In addition,
cytoplasmic c-Fos associates to the endoplasmic reticulum
(ER) membranes and activates phospholipid synthesis
during cell growth and differentiation. Herein, it is shown
that in T98G cells, c-Fos/ER association and consequently
phospholipid synthesis activation is regulated by
the phosphorylated state of c-Fos tyrosine (tyr) residues.
The small amount of c-Fos present in quiescent T98G cells
is tyr-phosphorylated and not ER-membrane bound. In
growing cells, it is dephosphorylated, associated to ER
membranes and promotes phospholipid synthesis activation.
Impairing tyr-dephosphorylation abrogates phospholipid
synthesis activation and reduces proliferation rates to
those of quiescent cells. Substitution of tyr residues 10, 30,
106 and 337 evidence tyr 10 and 30 as relevant for this
regulatory phenomenon. It is concluded that phosphorylation
of tyr residues 10 and 30 of c-Fos regulate the rate
of synthesis of phospholipids by regulating c-Fos/ER
association.
dependent gene transcription responses. In addition,
cytoplasmic c-Fos associates to the endoplasmic reticulum
(ER) membranes and activates phospholipid synthesis
during cell growth and differentiation. Herein, it is shown
that in T98G cells, c-Fos/ER association and consequently
phospholipid synthesis activation is regulated by
the phosphorylated state of c-Fos tyrosine (tyr) residues.
The small amount of c-Fos present in quiescent T98G cells
is tyr-phosphorylated and not ER-membrane bound. In
growing cells, it is dephosphorylated, associated to ER
membranes and promotes phospholipid synthesis activation.
Impairing tyr-dephosphorylation abrogates phospholipid
synthesis activation and reduces proliferation rates to
those of quiescent cells. Substitution of tyr residues 10, 30,
106 and 337 evidence tyr 10 and 30 as relevant for this
regulatory phenomenon. It is concluded that phosphorylation
of tyr residues 10 and 30 of c-Fos regulate the rate
of synthesis of phospholipids by regulating c-Fos/ER
association.
0 to S phase transition leading to AP-1-
dependent gene transcription responses. In addition,
cytoplasmic c-Fos associates to the endoplasmic reticulum
(ER) membranes and activates phospholipid synthesis
during cell growth and differentiation. Herein, it is shown
that in T98G cells, c-Fos/ER association and consequently
phospholipid synthesis activation is regulated by
the phosphorylated state of c-Fos tyrosine (tyr) residues.
The small amount of c-Fos present in quiescent T98G cells
is tyr-phosphorylated and not ER-membrane bound. In
growing cells, it is dephosphorylated, associated to ER
membranes and promotes phospholipid synthesis activation.
Impairing tyr-dephosphorylation abrogates phospholipid
synthesis activation and reduces proliferation rates to
those of quiescent cells. Substitution of tyr residues 10, 30,
106 and 337 evidence tyr 10 and 30 as relevant for this
regulatory phenomenon. It is concluded that phosphorylation
of tyr residues 10 and 30 of c-Fos regulate the rate
of synthesis of phospholipids by regulating c-Fos/ER
association.