Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase.

Erickson, A. E.; Payne, D. Michael; Martino, Paul A.; Rossomando, Anthony; Shabanowitz, Jeffrey; Weber, Michael J.; Hunt, Donald F.; Sturgill, Thomas W.

doi:10.1016/s0021-9258(17)45433-0

Cited by 237 publications

(21 citation statements)

References 32 publications

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“…If this is the case, and if ERK1/ ERK2 no longer recognize Ser31 in hTH2, it would imply that the small insertion in hTH2 causes a switch in kinase specificity. In PC12 cell cultures, ERK activity (measured with the known ERK substrate myelin basic protein 292 ) and the ERK-dependent phosphorylation of Ser31 is activated by NGF, bradykinin, and various other treatments. In Swiss 3T3 cells, a fibroblast-derived cell line, EGF stimulated ERK activity.…”

Section: Neural Activity and Itsmentioning

confidence: 99%

Pterin-Dependent Amino Acid Hydroxylases

1996

Chem. Rev.

314

385

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Section: Neural Activity and Itsmentioning

confidence: 99%

Pterin-Dependent Amino Acid Hydroxylases

1996

Chem. Rev.

314

385

View full text Add to dashboard Cite

“…The posttranslational modification of proteins has acquired increasing importance as their role in signal transduction and influence on protein conformation has been discerned. Myelin basic protein has been shown to be an effective substrate for mitogen-activated protein kinase (MAPK) (16). The MAP kinase cascade is conserved in all eukaryotes, and thus, the ability of MBP to function as a substrate may be indicative of its role in a signal transduction pathway.…”

mentioning

confidence: 99%

“…The use of mass spectrometry to identify some of the amino acid residues of bovine MBP that are phosphorylated in vitro by MAP kinase was reported by Erickson et al (16). Gibson et al (20) subjected the human MBP peptide fragment 45-89 to mass spectral analysis and were unable to confirm the phosphorylation of Ser 56.…”

mentioning

confidence: 99%

Determination of the Sites of Posttranslational Modifications in the Charge Isomers of Bovine Myelin Basic Protein by Capillary Electrophoresis-Mass Spectroscopy

Zand

Jin

et al. 1998

Biochemistry

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The posttranslational modifications in each of the 18.5 kDa bovine myelin basic protein charge isomers C-1 to C-6 have been determined by the use of capillary electrophoresis-mass spectroscopy. The pattern of modifications is viewed as being unique to each charge isomer and is thought to reflect a specific placement and function for each isomer in the myelin membrane. Several of the sites of posttranslational phosphorylation were found to differ from a number of the reported sites that were phosphorylated in vitro by various kinases. These differences suggest that an extremely cautious approach be taken in identifying in vivo posttranslationally modified amino acid residues from residues that have been modified in vitro by various kinases. We have identified the following posttranslationally phosphorylated and deamidated, modified sites in the bovine MBP components C1-C6. C1 has no modification; C2 represents a deamidation of Gln 146; in C3, Thr 97 and Ser 164 are phosphorylated; in C4, Ser 54, Thr 97, and Ser 160 are phosphorylated; in C5 Ser 7, Ser 54, Thr 97, and Ser 164 are phosphorylated; and in C6, Ser 7, Ser 54, Thr 97, Ser 160, and Ser 164 are phosphorylated.

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“…Each phosphorylated peptide was scraped off the cellulose plate, eluted with pH 1.9 electrophoresis buffer (12), covalently attached to an aryl amine-derivatized membrane (Millipore, Bedford, Mass. ), and subjected to repetitive cycles of Edman degradation as described previously (12,35).…”

Section: Methodsmentioning

confidence: 99%

Mitogen-Activated Protein Kinase Kinase 1 (MKK1) Is Negatively Regulated by Threonine Phosphorylation

Rossomando

Dent

Sturgill

et al. 1994

Molecular and Cellular Biology

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Mitogen-activated protein kinase kinase 1 (MKK1), a dual-specificity tyrosine/threonine protein kinase, has been shown to be phosphorylated and activated by the raf oncogene product as part of the mitogen-activated protein kinase cascade. Here we report the phosphorylation and inactivation of MKK1 by phosphorylation on threonine 286 and threonine 292. MKK1 contains a consensus phosphorylation site for p34cdc2, a serine/threonine protein kinase that regulates the cell division cycle, at Thr-286 and a related site at Thr-292. p34cdc2 catalyzes the in vitro phosphorylation of MKK1 on both of these threonine residues and inactivates MKK1 enzymatic activity. Both sites are phosphorylated in vivo as well. The data presented in this report provide evidence that MKK1 is negatively regulated by threonine phosphorylation.

show abstract

Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase.

Cited by 237 publications

References 32 publications

Pterin-Dependent Amino Acid Hydroxylases

Pterin-Dependent Amino Acid Hydroxylases

Determination of the Sites of Posttranslational Modifications in the Charge Isomers of Bovine Myelin Basic Protein by Capillary Electrophoresis-Mass Spectroscopy

Mitogen-Activated Protein Kinase Kinase 1 (MKK1) Is Negatively Regulated by Threonine Phosphorylation

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