Phosphorylation on basic amino acids in myelin basic protein

Smith, Larry Scott; Kern, Carl W.; Halpern, Richard M.; Smith, Rhona

doi:10.1016/0006-291x(76)90809-3

Cited by 53 publications

(23 citation statements)

References 9 publications

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“…However, almost all other studies in eukaryotes have focused on the phosphorylation of serine, threonine and tyrosine residues since partial acid hydrolysis, as used for conventional phosphoamino acid analysis, destroys the phosphoramidate bonds found in phosphohistidine, phospholysine or phosphoarginine [7]. Phosphoramidate bonds and protein kinases that phosphorylate arginine, histidine or lysine have been reported in eukaryotes [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] and reviewed recently [26]. Saccharomyces cerevisiae contains a kinase that transfers phosphate from ATP to histidine-75 in the protein, histone H4, in vitro [27].…”

Section: Introductionmentioning

confidence: 99%

Protein histidine phosphatase activity in rat liver and spinach leaves

Matthews

MacKintosh

1995

FEBS Letters

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Whole cell extracts from rat liver or spinach leaves contain divalent ion-independent protein histidine phosphatase activity due to phosphatases of the PPIlPP2A family. In the rat liver extract, almost all the activity was found in the PP1, PP2A~ and PP2A2 peaks. In the spinach leaf extract, four phosphorylase phosphatase activity peaks were resolved --three containing PP1 and one containing PP2A --and all showed histidine phosphatase activity. Thus, protein histidine phosphatase activity is expressed in the cytosolic forms of protein phosphatases of the PPIlPP2A family in mammalian and plant cells.

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Section: Introductionmentioning

confidence: 99%

Protein histidine phosphatase activity in rat liver and spinach leaves

Matthews

MacKintosh

1995

FEBS Letters

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confidence: 99%

“…In a solution circular dichroism (CD) and Fourier transform infrared spectroscopic study, MBP peptides from this region were found to have both ␣-helix and ␤-sheet structures in methanol, with the latter increasing in amount in progressively shorter peptides (17). The crystal structures of peptides 85-99 and 86 -105 bound to class II MHC proteins have been found to be extended (18,19).We have previously used site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) spectroscopy (20,21) to compare the membrane interactions of normal murine MBP (mMBP) with that of a less cationic form that predominates in MS (22). In that study, H85R1 was found to be motionally restricted, yet situated more than 3 Å above the lipid phosphate groups.…”

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confidence: 99%

An Immunodominant Epitope of Myelin Basic Protein Is an Amphipathic α-Helix

Bates

Feix

Boggs

et al. 2004

Journal of Biological Chemistry

124

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Myelin basic protein is a candidate autoantigen in multiple sclerosis. One of its dominant antigenic epitopes is segment Pro 85 to Pro 96 (human sequence numbering, corresponding to Pro 82 to Pro 93 in the mouse). There have been several, contradictory predictions of secondary structure in this region; either ␤-sheet, ␣-helix, random coil, or combinations thereof have all been proposed. In this paper, molecular dynamics and site-directed spin labeling in aqueous solution indicate that this segment forms a transient ␣-helix, which is stabilized in 30% trifluoroethanol. When bound to a myelin-like membrane surface, this antigenic segment exhibits a depth profile that is characteristic of an amphipathic ␣-helix, penetrating up to 12 Å into the bilayer. The ␣-helix is tilted ϳ9°, and the central lysine is in an ideal snorkeling position for side-chain interaction with the negatively charged phospholipid head groups.Multiple sclerosis (MS) 1 is thought to be an autoimmune disease characterized by chronic inflammatory response against myelin in the central nervous system. There is significant evidence that myelin basic protein (MBP) is a candidate antigen for T-cells and autoantibodies in MS (1). The 18.5-kDa isoform of MBP maintains the compaction of the myelin sheath in the central nervous system by anchoring the cytoplasmic face of the two apposing bilayers (2, 3). The mechanism and sites that are important for membrane adhesion are not known.The level of anti-MBP antibodies is increased in the cerebrospinal fluid of patients with active MS (4), as well as in 96% of patients with relapsing and chronic MS (5). An MBP region between Pro 85 and Pro 96 (human sequence numbering) was identified to be a minimal B cell epitope and a T cell epitope for HLA DR2b (DRB1*1501)-restricted T cells that recognize the protein (1, 6). This epitope overlaps with the DR2a-restricted epitope for T-cells reactive to MBP residues 87-106 (7). Experimental treatments for MS based on peptide mimetics of MBP have focused on this region of the protein (8).In solution, MBP is "intrinsically unstructured" (or "natively unfolded") (9). Upon binding to detergents or lipids, the levels of ␤-sheet and especially ␣-helical structure increase dramatically (10, 11). Presently the tertiary structure of MBP is unknown, with the most detailed predictions coming from Martenson (12) and Stoner (13) in the mid-1980s. In these models, as well as in a newer model based upon further research on an electron microscopy single-particle reconstruction, residues 86 -92 are found in a ␤-sheet (14, 15). Using [ 1 H]NMR and circular dichroic spectropolarimetry of various MBP peptides with detergent micelles, Mendz et al. (16) suggested that there were discrete interaction sites in the protein, one of which could be a helix between residues 87 and 97. Based on the arrangement of hydrophobic and hydrophilic residues, Warren et al. (6) predicted that this epitope of MBP was an amphipathic ␣-helix located at the interface between the oligodendrocyte cytoplasm and the me...

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“…5B, lane massie staining of all proteins was recovered upon the return to low pH. This alkali lability of phosphorylation suggested that histidine, lysine, arginine (20,21), or tyrosine phosphates were insignificant constituents of labeled ppl 8. Treatment of labeled pp 18, prior to SDS-PAGE, with 100 mm hydroxylamine failed to eliminate the attached phosphate.…”

Section: Highly Purified Ppl8 Autophosphorylates On Serine Residuesmentioning

confidence: 90%

Rapid Cycling of Autophosphorylation of a Ca²⁺-Calmodulin Regulated Plasma Membrane Located Protein Kinase from Pea

Blowers¹,

Trewavas²

1989

Plant Physiol.

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Plasma membrane vesicles from pea (Pisum sativum L.) seedlings contain an autophosphorylating calcium-activated protein kinase of relative molecular weight 18,000 (phosphoprotein 18, pp18). Pulse chase analysis revealed that pp18 autophosphorylation exhibited very rapid tumover. pp18 was the only detectable plasma membrane protein to have this property. pp18 has been highly purified by affinity chromatography and the final preparation contains peptides of relative molecular weight 67,000,48,000, and 18,000. Highly purified pp18 still showed rapid cycling of autophosphorylated phosphate attached to pp18. Tumover of pp18 autophosphorylation was accelerated by ADP, but this effect did not appear to be the back reaction of the kinase since inorganic phosphate accumulation is increased by ADP. A rapid cycling of phosphorylation is an ideal control point in signal transduction.

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Phosphorylation on basic amino acids in myelin basic protein

Cited by 53 publications

References 9 publications

Protein histidine phosphatase activity in rat liver and spinach leaves

Protein histidine phosphatase activity in rat liver and spinach leaves

An Immunodominant Epitope of Myelin Basic Protein Is an Amphipathic α-Helix

Rapid Cycling of Autophosphorylation of a Ca²⁺-Calmodulin Regulated Plasma Membrane Located Protein Kinase from Pea

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Phosphorylation on basic amino acids in myelin basic protein

Cited by 53 publications

References 9 publications

Protein histidine phosphatase activity in rat liver and spinach leaves

Protein histidine phosphatase activity in rat liver and spinach leaves

An Immunodominant Epitope of Myelin Basic Protein Is an Amphipathic α-Helix

Rapid Cycling of Autophosphorylation of a Ca2+-Calmodulin Regulated Plasma Membrane Located Protein Kinase from Pea

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Rapid Cycling of Autophosphorylation of a Ca²⁺-Calmodulin Regulated Plasma Membrane Located Protein Kinase from Pea