Phosphorylation of multiple proteins of both ribosomal subunits in rat cerebral cortex <i>in vivo</i>. Effect of adenosine 3′:5′-cyclic monophosphate

Roberts, Sidney; Morelos, Beatrice S.

doi:10.1042/bj1840233

Cited by 20 publications

(30 citation statements)

References 44 publications

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“…More specifically, prolonged exposure of the electrophoretograms to radioautography (10-15 days) revealed that cerebral ribosomal proteins with the electrophoretic properties of S3a, S2, and S5 were phosphorylated in vivo. 17 In addition, it was further suggested that rpS2 phosphorylation may be restricted to polyribosomes, whereas rpS3a and rpS5 may become phosphorylated only in free ribosomal subunits. 17,18 However, experiments reported by Roberts and Ashby 26 corroborate the in vitro phosphorylation of ribosomal proteins S2, S3, and S6 but not the phosphorylation of rpS5.…”

Section: Experimental Evidence Of Rps5 Phosphorylationmentioning

confidence: 99%

On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli

Matragkou

Papachristou

Karetsou

et al. 2009

Journal of Molecular Biology

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Section: Experimental Evidence Of Rps5 Phosphorylationmentioning

confidence: 99%

On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli

Matragkou

Papachristou

Karetsou

et al. 2009

Journal of Molecular Biology

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“…Thus regulatory factors governing the activation of protease-activated kinase I must be identified before phosphorylation of this protein can be demonstrated in reticulocytes. Limited phosphorylation of S10 has been observed in brain [37]; this phosphorylation was not stimulated by CAMP or analogues of CAMP.…”

Section: -I +Imentioning

confidence: 98%

Phosphorylation of 40‐S Ribosomal Subunits by cAMP‐Dependent, cGMP‐Dependent and Protease‐Activated Protein Kinases

Grande

Traugh

1982

European Journal of Biochemistry

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The phosphorylation of 40-S ribosomal subunits by cyclic-nucleotide-dependent and protease-activated protein kinases from rabbit reticulocytes was studied in vitro. Under optimal conditions the CAMP-dependent protein kinases incorporated up to 2 mol phosphate/mol S6. The electrophoretic mobility of S6 following phosphorylation indicated that this value was not an average for a population of maximally phosphorylated and non-phosphorylated S6 but represented a uniform population of diphosphorylated 40-S ribosomal subunits. Tryptic digests of S6 were analyzed by two-dimensional fingerprinting following phosphorylation with the CAMP-dependent protein kinase; two phosphopeptides, A and B, were observed. When 40-S ribosomal subunits were examined with the cGMP-dependent protein kinase, 1 mol phosphate was incorporated/mol S6. Upon analysis of the phosphopeptides obtained with the cGMP-dependent protein kinase, only peptide A was observed. S6 was also modified by a cyclic-nucleotide-independent protein kinase, protease-activated kinase 11, following activation of the enzyme by limited proteolytic digestion. These findings suggest that a multiple protein kinase system may regulate the phosphorylation-state of S6. A second ribosomal protein, S10, was phosphorylated by a different cyclic-nucleotide-independent protein kinase, protease-activated kinase I, and up to 1 mol phosphate was incorporated.

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“…The intracisternal route was selected because only very small amounts of radioactivity were incorporated into brain ribosomal proteins when [32pIpi was given intraperitoneally or intravenously. This intracisternal procedure had no discernible effect on patterns of cerebral ribosomal proteins obtained by two-dimensional electrophoresis (Roberts & Morelos, 1979) or on the sedimentation properties of purified cerebral ribosomes (Roberts & Morelos, 1976). The animals were routinely killed by decapitation.…”

Section: Treatment Ofanimalsmentioning

confidence: 85%

“…The 60S subunits were re-dissociated and re-fractionated as described above to remove contaminating 80S ribosomes and 40S subunits. Cerebral 40S and 60S subunits isolated by this procedure appeared to be virtually free of cross-contamination and nonribosomal phosphorylated proteins (Roberts & Ashby, 1978;Roberts & Morelos, 1979).…”

Section: Preparation Of Cerebral Ribosomes and Ribosomal Subunitsmentioning

confidence: 99%

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Cerebral ribosomal protein phosphorylation in experimental hyperphenylalaninaemia

Roberts¹,

Morelos²

1980

Biochemical Journal

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Investigations were carried out on the effects of phenylalanine loading on ribosomal protein phosphorylation in cerebral cortices of infant rats. Administration of L-phenylalanine intraperitoneally, in doses of 1 or 2 mg/g body wt., resulted within 30 min in a significant decrease in incorporation of radioactivity from intracisternally administered [32P]Pi into constitutive ribosomal proteins of the cerebral 40S subunit. This phenomenon was not accompanied by significant variations in 32P uptake into the cerebral cytosol. Incorporation of radioactivity into ribosomal proteins of the cerebral 60S subunit exhibited only minor variations under these circumstances. Alterations in the phosphorylation state of cerebral 40S ribosomal proteins induced by phenylalanine loading involved principally the S6 protein, which exists in multiple states of phosphorylation. The proportions of the more highly phosphorylated congeners of this protein were markedly decreased, as detected by two-dimensional electrophoretograms and autoradiographs of the cerebral 40S ribosomal proteins. Phenylalanine loading also altered the relative extent of phosphorylation of the S6 protein in cerebral polyribosomes and monoribosomes. In control animals, the specific radioactivity of 40S proteins in cerebral polyribosomes was five to ten times that of 40S proteins in the monoribosome population. At 1 h after phenylalanine administration, the specific radioactivities of 40S proteins in the two ribosome populations tended to approach equality. These alterations in ribosomal protein phosphorylation were accompanied by a decrease in the proportion of polyribosomes in purified ribosome preparations isolated from cerebral cortices of phenylalanine-treated infant rats. In animals given the higher dose of phenylalanine (2 mg/g body wt.), subsequent administration of a mixture of seven neutral amino acids, which resulted in partial recovery of polyribosomes, also tended to reverse the changes in ribosomal protein phosphorylation. Variations in the activities of ribonuclease enzymes in the cerebral cytosol were also observed under these conditions. Administration of phenylalanine increased the activities of cerebral ribonucleases, whereas subsequent treatment with the amino acid mixture partly reversed this effect. The results suggest that alterations in cerebral ribosomal protein phosphorylation, ribosome aggregation and ribosome function are interrelated in experimental hyperphenylalaninaemia.

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Phosphorylation of multiple proteins of both ribosomal subunits in rat cerebral cortex in vivo. Effect of adenosine 3′:5′-cyclic monophosphate

Cited by 20 publications

References 44 publications

On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli

On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli

Phosphorylation of 40‐S Ribosomal Subunits by cAMP‐Dependent, cGMP‐Dependent and Protease‐Activated Protein Kinases

Cerebral ribosomal protein phosphorylation in experimental hyperphenylalaninaemia

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