Localization of Endogenous Phosphoserine Residues in the Primary Structure of Proteins

Meyer, Helmut E.; Kuhn, Carl C.; Meyer, G. F.; Swiderek, Kristine M.; Weber, Carsten; Hoffmann-Posorske, Edeltraut; Korte, H.; Heilmeyer, Ludwig

doi:10.1007/978-3-642-73834-0_4

Cited by 5 publications

(7 citation statements)

References 3 publications

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“…PTH-serine indicates that a phosphorylated serine was at this position as previously described for other phosphoproteins [23]. For lamin C this indicates that Ser 39-', Ser 4°9, and possibly Ser ':°7 are partially phosphorylated in interphase.…”

Section: Peptme Purification and Sequencotgsupporting

confidence: 57%

“…The sequence information was used to identify putative phosphorylation sites in interphase lamin C and following in vitro phosphorylation. Alterations in PTH-serine/PTH-DTT-dehydroalanine ratios were determined to identify phosphoserine residues as previously described [23]. Sufficient quantities of purified lamins allowed us to recover on average 150 pmol of lamin C pcptides for direct sequence analysis.…”

Section: Discussionmentioning

confidence: 99%

“…However, for these peptides the phosphorylated Sequence analysis of RP-HPLC separated radioactive peaks, following lamin C phosphorylation with cdc2-kinase (A), PKC (B) and PKA (C). The peptides were assigned to the sequence of the whole lamin C protein deduced from eDNA analysis [23]. S n no serine but increase of PTH-DTT-deb.odroalanine detected in this position, compared to previous step of Edman degradation.…”

Section: Hplc-analysis Of Lys-c Digested Lamin C Phospho-mentioning

confidence: 99%

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Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing

Eggert

Radomski

Tripier³

et al. 1991

FEBS Letters

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Isolated interphase lamin C, obtained from Ehrlich ascites tumor cells, was digested by Lys-C endoproteinase, the resulting peptides separated by reversed-phase HPLC and subjected to microsequencing in order to identify phosphorylation sites in interphase and following phosphorylation in vitro by cdc2-kinase, protein kinase C (PKC) and protein kinase A (PKA), respectively. Nuclear lamin C showed partial phosphorylation of Ser ~9~' and Ser ~m, and possibly Ser 4°7 in interphase. Phosphorylation was increased in response to cdc2-kinase at Ser 39° and Ser ~: and to PKC at Ser 57-'. The N-terminal peptide (aa 1-32) containing consensus sequences for the 3 kinases was phosphorylated by cde2-kinase, PKC and PKA. The sequence data suggests that multiple mr~leeular switches via lamina modification control the dynamic behaviour of the nucleoskeleton during the cell cycle.

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Section: Peptme Purification and Sequencotgsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Section: Hplc-analysis Of Lys-c Digested Lamin C Phospho-mentioning

confidence: 99%

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Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing

Eggert

Radomski

Tripier³

et al. 1991

FEBS Letters

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“…The phosphate group of phosphothreonine is eliminated completely during the Edman degradation process, like the phosphate group of phosphoserine [24,25]. Therefore, the amount of DTT-addition products of the dehydroaminobutyric acid is increased compared with an unphosphorylated threonine.…”

Section: Discussionmentioning

confidence: 99%

N‐terminal sequence analysis of the 8 kDa protein inChlamydomonas reinhardiiLocalization of the phosphothreonine

Dedner

Meyer

Ashton³

et al. 1988

FEBS Letters

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A phosphorylated 8 kDa protein of Chlamydomonas reinhurdii thylakoids has been isolated and its N-terminal amino acid sequence determined by gas-phase sequencing. The sequence analysis of the 48 amino acid residues revealed that this protein is about 50% homologous to the psb H gene products of higher plants. In contrast to them, it contains an insert of seven amino acid residues (Ser-5 to Lys-1 1). The first threonine residue was phosphorylated as determined by 32P detection during sequencing and also by analysis of the modified degradation products in the chemical reaction of the Edman degradation process. This latter method allows the identification of phosphorylated threonine residues without radiolabelling the protein. (Chlamydomonus reinhardiz)

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“…The sequence analysis of the peptides was performed using a 477A pulsed liquid phase protein/ peptide sequencer and a 120A on-line PTH amino acid analyser (Applied Biosystems). Phosphoserines were identified by gas phase sequencing, making use of the formation of the dithiothreitol adduct of dehydroalanine from serine phosphate (Meyer et al, 1990).…”

Section: Sequencing Of Phosphorylated Peptidesmentioning

confidence: 99%

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region.

et al. 1992

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Localization of Endogenous Phosphoserine Residues in the Primary Structure of Proteins

Cited by 5 publications

References 3 publications

Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing

Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing

N‐terminal sequence analysis of the 8 kDa protein inChlamydomonas reinhardiiLocalization of the phosphothreonine

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region.

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Localization of Endogenous Phosphoserine Residues in the Primary Structure of Proteins

Cited by 5 publications

References 3 publications

Identification of phosphorylation sites on murine nuclear lamin C by RP&#x2010;HPLC and microsequencing

Identification of phosphorylation sites on murine nuclear lamin C by RP&#x2010;HPLC and microsequencing

N‐terminal sequence analysis of the 8 kDa protein inChlamydomonas reinhardiiLocalization of the phosphothreonine

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region.

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Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing

Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing