Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation

Mohammed Filali, Shiyong Li, Ha Won Kim, Brian Wadzinski, Malek Kamoun

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

We have identified a 36 kD phosphoprotein that forms a complex with spliceosomal small nuclear ribonucleoproteins in lymphocyte extracts. This 36 kD protein is differentially phosphorylated in transformed human lymphoid cell lines and is regulated by IL-2 in peripheral blood T cells. We purified the 36 kD protein from human lymphocytes by employing a combination of immuno-affinity chromatography and preparative two-dimensional gel electrophoresis. Internal amino acid sequence analysis of the purified protein yielded two peptides that had perfect matches with sequences in the human protein serine/threonine phosphatase 6 (PP6). Using degenerate primers corresponding to the peptides, we obtained from a human T lymphocyte cDNA library a DNA fragment whose sequence is homologous to an EST cDNA clone (R05547). The predicted amino acid sequence of this clone showed over 98% sequence identity to human PP6. The identification of an IL-2 regulated type 6 protein serine/threonine phosphatase in lymphocytes was further substantiated by immunoblotting with anti-peptide antibodies. These findings suggest that PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL-2 receptor stimulation.

Original languageEnglish (US)
Pages (from-to)153-163
Number of pages11
JournalJournal of Cellular Biochemistry
Volume73
Issue number2
DOIs
StatePublished - May 1 1999
Externally publishedYes

Fingerprint

Lymphocytes
Phosphoric Monoester Hydrolases
Interleukin-2
T-cells
Phosphoprotein Phosphatases
Peptides
Cells
Small Nuclear Ribonucleoproteins
Affinity chromatography
Amino Acids
Proteins
Interleukin-2 Receptors
Phosphoproteins
Expressed Sequence Tags
Electrophoresis
Gene Library
Clone Cells
Blood
T-Lymphocytes
Complementary DNA

Keywords

  • Cell cycle regulation
  • Cellular activation
  • IL2 receptor
  • Protein ser/thr phosphatase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation. / Filali, Mohammed; Li, Shiyong; Kim, Ha Won; Wadzinski, Brian; Kamoun, Malek.

In: Journal of Cellular Biochemistry, Vol. 73, No. 2, 01.05.1999, p. 153-163.

Research output: Contribution to journalArticle

Filali, Mohammed ; Li, Shiyong ; Kim, Ha Won ; Wadzinski, Brian ; Kamoun, Malek. / Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation. In: Journal of Cellular Biochemistry. 1999 ; Vol. 73, No. 2. pp. 153-163.
@article{74d89e6ae6864fdcbf87600c4c03b941,
title = "Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation",
abstract = "We have identified a 36 kD phosphoprotein that forms a complex with spliceosomal small nuclear ribonucleoproteins in lymphocyte extracts. This 36 kD protein is differentially phosphorylated in transformed human lymphoid cell lines and is regulated by IL-2 in peripheral blood T cells. We purified the 36 kD protein from human lymphocytes by employing a combination of immuno-affinity chromatography and preparative two-dimensional gel electrophoresis. Internal amino acid sequence analysis of the purified protein yielded two peptides that had perfect matches with sequences in the human protein serine/threonine phosphatase 6 (PP6). Using degenerate primers corresponding to the peptides, we obtained from a human T lymphocyte cDNA library a DNA fragment whose sequence is homologous to an EST cDNA clone (R05547). The predicted amino acid sequence of this clone showed over 98{\%} sequence identity to human PP6. The identification of an IL-2 regulated type 6 protein serine/threonine phosphatase in lymphocytes was further substantiated by immunoblotting with anti-peptide antibodies. These findings suggest that PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL-2 receptor stimulation.",
keywords = "Cell cycle regulation, Cellular activation, IL2 receptor, Protein ser/thr phosphatase",
author = "Mohammed Filali and Shiyong Li and Kim, {Ha Won} and Brian Wadzinski and Malek Kamoun",
year = "1999",
month = "5",
day = "1",
doi = "10.1002/(SICI)1097-4644(19990501)73:2<153::AID-JCB2>3.0.CO;2-7",
language = "English (US)",
volume = "73",
pages = "153--163",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley-Liss Inc.",
number = "2",

}

TY - JOUR

T1 - Identification of a type 6 protein ser/thr phosphatase regulated by interleukin-2 stimulation

AU - Filali, Mohammed

AU - Li, Shiyong

AU - Kim, Ha Won

AU - Wadzinski, Brian

AU - Kamoun, Malek

PY - 1999/5/1

Y1 - 1999/5/1

N2 - We have identified a 36 kD phosphoprotein that forms a complex with spliceosomal small nuclear ribonucleoproteins in lymphocyte extracts. This 36 kD protein is differentially phosphorylated in transformed human lymphoid cell lines and is regulated by IL-2 in peripheral blood T cells. We purified the 36 kD protein from human lymphocytes by employing a combination of immuno-affinity chromatography and preparative two-dimensional gel electrophoresis. Internal amino acid sequence analysis of the purified protein yielded two peptides that had perfect matches with sequences in the human protein serine/threonine phosphatase 6 (PP6). Using degenerate primers corresponding to the peptides, we obtained from a human T lymphocyte cDNA library a DNA fragment whose sequence is homologous to an EST cDNA clone (R05547). The predicted amino acid sequence of this clone showed over 98% sequence identity to human PP6. The identification of an IL-2 regulated type 6 protein serine/threonine phosphatase in lymphocytes was further substantiated by immunoblotting with anti-peptide antibodies. These findings suggest that PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL-2 receptor stimulation.

AB - We have identified a 36 kD phosphoprotein that forms a complex with spliceosomal small nuclear ribonucleoproteins in lymphocyte extracts. This 36 kD protein is differentially phosphorylated in transformed human lymphoid cell lines and is regulated by IL-2 in peripheral blood T cells. We purified the 36 kD protein from human lymphocytes by employing a combination of immuno-affinity chromatography and preparative two-dimensional gel electrophoresis. Internal amino acid sequence analysis of the purified protein yielded two peptides that had perfect matches with sequences in the human protein serine/threonine phosphatase 6 (PP6). Using degenerate primers corresponding to the peptides, we obtained from a human T lymphocyte cDNA library a DNA fragment whose sequence is homologous to an EST cDNA clone (R05547). The predicted amino acid sequence of this clone showed over 98% sequence identity to human PP6. The identification of an IL-2 regulated type 6 protein serine/threonine phosphatase in lymphocytes was further substantiated by immunoblotting with anti-peptide antibodies. These findings suggest that PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL-2 receptor stimulation.

KW - Cell cycle regulation

KW - Cellular activation

KW - IL2 receptor

KW - Protein ser/thr phosphatase

UR - http://www.scopus.com/inward/record.url?scp=0033135523&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033135523&partnerID=8YFLogxK

U2 - 10.1002/(SICI)1097-4644(19990501)73:2<153::AID-JCB2>3.0.CO;2-7

DO - 10.1002/(SICI)1097-4644(19990501)73:2<153::AID-JCB2>3.0.CO;2-7

M3 - Article

VL - 73

SP - 153

EP - 163

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 2

ER -