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PMID: 1648233 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 13 ·1991-07-01 ·Pages 5867-71

Gu MX, York JD, Warshawsky I, Majerus PW

Abstract

We have isolated a cDNA encoding a third type of protein-tyrosine-phosphatase. We screened human megakaryoblastic cell line (MEG-01) an umbilical vein endothelial cell cDNA libraries to obtain a 3.7-kilobase cDNA designated PTPase MEG. Northern blot analysis of MEG-01 RNA detected a 3.7-kilobase transcript, suggesting that a full-length cDNA has been identified. PTPase MEG cDNA contains an open reading frame of 926 amino acids. The cDNA has a G+C-rich 5' untranslated region of 771 nucleotides that has the potential to form stable stem-loop structures and has two upstream ATG codons. The predicted protein (Mr = 105,910) has no apparent membrane-spanning region and contains a single protein-tyrosine-phosphatase domain (amino acids 659-909) that is 35-40% identical to previously described tyrosine-phosphatase domains. The recombinant phosphatase domain possesses protein-tyrosine-phosphatase activity when expressed in Escherichia coli. The amino-terminal region (amino acids 31-367) is 45% identical to the amino terminus of human erythrocyte protein 4.1, a cytoskeletal protein. The identification of a protein-tyrosine-phosphatase that is related to cytoskeletal proteins implies that cell signaling activities reside not only in transmembrane receptors but in cytoskeletal elements as well.

MeSH Terms
Amino Acid Sequence Base Sequence Blotting, Northern Cloning, Molecular Cytoskeletal Proteins/chemistry Cytosol/enzymology DNA/genetics Escherichia coli Gene Expression Humans Megakaryocytes/enzymology Membrane Proteins/chemistry Molecular Sequence Data Neuropeptides Oligonucleotides/chemistry Phosphoprotein Phosphatases/genetics,metabolism Polymerase Chain Reaction Protein Tyrosine Phosphatase, Non-Receptor Type 4 Protein Tyrosine Phosphatases/genetics,metabolism RNA, Messenger/genetics Recombinant Proteins/metabolism Restriction Mapping
Chemicals
Cytoskeletal Proteins Membrane Proteins Neuropeptides Oligonucleotides RNA, Messenger Recombinant Proteins erythrocyte membrane band 4.1 protein erythrocyte membrane protein band 4.1-like 1 DNA Phosphoprotein Phosphatases PTPN4 protein, human Protein Tyrosine Phosphatase, Non-Receptor Type 4 Protein Tyrosine Phosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gu M X
Washington University School of Medicine, Division of Hematology-Oncology, St. Louis, MO 63110.
York J D
Warshawsky I
Majerus P W
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.13.5867
Published
1991-07-01
Pages
5867-71
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC51979
Subset
IM
Grants
NHLBI NIH HHS · HL07088 · United States
NHLBI NIH HHS · HL14147 · United States
NHLBI NIH HHS · HL16634 · United States
Databases
GENBANK
M59224, M59225, M59226, M60611, M63333, M63334, M64653, M68941, M68958, M74488
External Links
PubMed source DOI: 10.1073/pnas.88.13.5867 PMC Full Text View journal details
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