O-sulfonation of serine and threonine

K. F. Medzihradszky, Z. Darula, E. Perlson, M. Fainzilber, R. J. Chalkley, H. Ball, D. Greenbaum, M. Bogyo, D. R. Tyson, R. A. Bradshaw, A. L. Burlingame

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

Protein sulfonation on serine and threonine residues is described for the first time. This post-translational modification is shown to occur in proteins isolated from organisms representing a broad span of eukaryote evolution, including the invertebrate mollusk Lymnaea stagnalis, the unicellular malaria parasite Plasmodium falciparum, and humans. Detection and structural characterization of this novel post-translational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and a myosin light chain from the snail, a cathepsin-C-like enzyme from the parasite, and the cytoplasmic domain of the human orphan receptor tyrosine kinase Ror-2. These findings suggest that sulfonation of serine and threonine may be involved in multiple functions including protein assembly and signal transduction.

Original languageEnglish (US)
Pages (from-to)429-443
Number of pages15
JournalMolecular and Cellular Proteomics
Volume3
Issue number5
DOIs
StatePublished - May 2004

Fingerprint

Sulfonation
Threonine
Serine
Post Translational Protein Processing
Parasites
Proteins
Cathepsin C
TYK2 Kinase
Lymnaea
Signal transduction
Myosin Light Chains
Intermediate Filaments
Falciparum Malaria
Mollusca
Liquid chromatography
Snails
Invertebrates
Tandem Mass Spectrometry
Eukaryota
Liquid Chromatography

ASJC Scopus subject areas

  • Biochemistry

Cite this

Medzihradszky, K. F., Darula, Z., Perlson, E., Fainzilber, M., Chalkley, R. J., Ball, H., ... Burlingame, A. L. (2004). O-sulfonation of serine and threonine. Molecular and Cellular Proteomics, 3(5), 429-443. https://doi.org/10.1074/mcp.M300140-MCP200

O-sulfonation of serine and threonine. / Medzihradszky, K. F.; Darula, Z.; Perlson, E.; Fainzilber, M.; Chalkley, R. J.; Ball, H.; Greenbaum, D.; Bogyo, M.; Tyson, D. R.; Bradshaw, R. A.; Burlingame, A. L.

In: Molecular and Cellular Proteomics, Vol. 3, No. 5, 05.2004, p. 429-443.

Research output: Contribution to journalArticle

Medzihradszky, KF, Darula, Z, Perlson, E, Fainzilber, M, Chalkley, RJ, Ball, H, Greenbaum, D, Bogyo, M, Tyson, DR, Bradshaw, RA & Burlingame, AL 2004, 'O-sulfonation of serine and threonine', Molecular and Cellular Proteomics, vol. 3, no. 5, pp. 429-443. https://doi.org/10.1074/mcp.M300140-MCP200
Medzihradszky KF, Darula Z, Perlson E, Fainzilber M, Chalkley RJ, Ball H et al. O-sulfonation of serine and threonine. Molecular and Cellular Proteomics. 2004 May;3(5):429-443. https://doi.org/10.1074/mcp.M300140-MCP200
Medzihradszky, K. F. ; Darula, Z. ; Perlson, E. ; Fainzilber, M. ; Chalkley, R. J. ; Ball, H. ; Greenbaum, D. ; Bogyo, M. ; Tyson, D. R. ; Bradshaw, R. A. ; Burlingame, A. L. / O-sulfonation of serine and threonine. In: Molecular and Cellular Proteomics. 2004 ; Vol. 3, No. 5. pp. 429-443.
@article{96ab1988e99d4f5c9aea7fb7dc46845c,
title = "O-sulfonation of serine and threonine",
abstract = "Protein sulfonation on serine and threonine residues is described for the first time. This post-translational modification is shown to occur in proteins isolated from organisms representing a broad span of eukaryote evolution, including the invertebrate mollusk Lymnaea stagnalis, the unicellular malaria parasite Plasmodium falciparum, and humans. Detection and structural characterization of this novel post-translational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and a myosin light chain from the snail, a cathepsin-C-like enzyme from the parasite, and the cytoplasmic domain of the human orphan receptor tyrosine kinase Ror-2. These findings suggest that sulfonation of serine and threonine may be involved in multiple functions including protein assembly and signal transduction.",
author = "Medzihradszky, {K. F.} and Z. Darula and E. Perlson and M. Fainzilber and Chalkley, {R. J.} and H. Ball and D. Greenbaum and M. Bogyo and Tyson, {D. R.} and Bradshaw, {R. A.} and Burlingame, {A. L.}",
year = "2004",
month = "5",
doi = "10.1074/mcp.M300140-MCP200",
language = "English (US)",
volume = "3",
pages = "429--443",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

TY - JOUR

T1 - O-sulfonation of serine and threonine

AU - Medzihradszky, K. F.

AU - Darula, Z.

AU - Perlson, E.

AU - Fainzilber, M.

AU - Chalkley, R. J.

AU - Ball, H.

AU - Greenbaum, D.

AU - Bogyo, M.

AU - Tyson, D. R.

AU - Bradshaw, R. A.

AU - Burlingame, A. L.

PY - 2004/5

Y1 - 2004/5

N2 - Protein sulfonation on serine and threonine residues is described for the first time. This post-translational modification is shown to occur in proteins isolated from organisms representing a broad span of eukaryote evolution, including the invertebrate mollusk Lymnaea stagnalis, the unicellular malaria parasite Plasmodium falciparum, and humans. Detection and structural characterization of this novel post-translational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and a myosin light chain from the snail, a cathepsin-C-like enzyme from the parasite, and the cytoplasmic domain of the human orphan receptor tyrosine kinase Ror-2. These findings suggest that sulfonation of serine and threonine may be involved in multiple functions including protein assembly and signal transduction.

AB - Protein sulfonation on serine and threonine residues is described for the first time. This post-translational modification is shown to occur in proteins isolated from organisms representing a broad span of eukaryote evolution, including the invertebrate mollusk Lymnaea stagnalis, the unicellular malaria parasite Plasmodium falciparum, and humans. Detection and structural characterization of this novel post-translational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and a myosin light chain from the snail, a cathepsin-C-like enzyme from the parasite, and the cytoplasmic domain of the human orphan receptor tyrosine kinase Ror-2. These findings suggest that sulfonation of serine and threonine may be involved in multiple functions including protein assembly and signal transduction.

UR - http://www.scopus.com/inward/record.url?scp=2642545646&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2642545646&partnerID=8YFLogxK

U2 - 10.1074/mcp.M300140-MCP200

DO - 10.1074/mcp.M300140-MCP200

M3 - Article

C2 - 14752058

AN - SCOPUS:2642545646

VL - 3

SP - 429

EP - 443

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 5

ER -