Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis

F W Quelle; Kazuya Shimoda; William Thierfelder; Carrie Fischer; A Kim; S M Ruben; John L Cleveland; Jacalyn H Pierce; A D Keegan; Keats Nelms

doi:10.1128/MCB.15.6.3336

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Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis

Journal article

Peer reviewed

Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis

F W Quelle, Kazuya Shimoda, William Thierfelder, Carrie Fischer, A Kim, S M Ruben, John L Cleveland, Jacalyn H Pierce, A D Keegan and Keats Nelms

Molecular and cellular biology, Vol.15(6), pp.3336-3343

06/1995

DOI: 10.1128/MCB.15.6.3336

PMCID: PMC230567

PMID: 7760829

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Abstract

By searching a database of expressed sequences, we identified a member of the signal transducers and activators of transcription (Stat) family of proteins. Human and murine full-length cDNA clones were obtained and sequenced. The sequence of the human cDNA was identical to the recently published sequence for interleukin-4 (IL-4)-Stat (J. Hou, U. Schindler, W.J. Henzel, T.C. Ho, M. Brasseur, and S. L. McKnight, Science 265:1701-1706, 1994), while the murine Stat6 amino acid and nucleotide sequences were 83 and 84% identical to the human sequences, respectively. Using Stat6-specific antiserum, we demonstrated that Stat6 is rapidly tyrosine phosphorylated following stimulation of appropriate cell lines with IL-4 or IL-3 but is not detectably phosphorylated following stimulation with IL-2, IL-12, or erythropoietin. In contrast, IL-2, IL-3, and erythropoietin induce the tyrosine phosphorylation of Stat5 while IL-12 uniquely induces the tyrosine phosphorylation of Stat4. Inducible tyrosine phosphorylation of Stat6 requires the membrane-distal region of the IL-4 receptor alpha chain. This region of the receptor is not required for cell growth, demonstrating that Stat6 tyrosine phosphorylation does not contribute to mitogenesis.

Phosphorylation

Amino Acid Sequence

Cell Line

Humans

Molecular Sequence Data

Transcription Factors - genetics

Interleukin-3 - pharmacology

STAT6 Transcription Factor

Transcription Factors - metabolism

Interleukin-4 - pharmacology

Animals

Mitosis - drug effects

Base Sequence

Cloning, Molecular

Trans-Activators - genetics

Trans-Activators - metabolism

Transcription Factors - isolation & purification

Mice

Sequence Analysis

Details

Title: Subtitle: Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis
Creators: F W Quelle - Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA
Kazuya Shimoda
William Thierfelder
Carrie Fischer
A Kim
S M Ruben
John L Cleveland
Jacalyn H Pierce
A D Keegan
Keats Nelms
Resource Type: Journal article
Publication Details: Molecular and cellular biology, Vol.15(6), pp.3336-3343
DOI: 10.1128/MCB.15.6.3336
PMID: 7760829
PMCID: PMC230567
NLM abbreviation: Mol Cell Biol
ISSN: 0270-7306
eISSN: 1098-5549
Publisher: United States
Grant note: R01 DK44158 / NIDDK NIH HHS P01 HL53749 / NHLBI NIH HHS P30 CA21765 / NCI NIH HHS
Language: English
Date published: 06/1995
Academic Unit: Neuroscience and Pharmacology; Internal Medicine
Record Identifier: 9984040575402771

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