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cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein.

cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Research Abstract Details 

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  • cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Abstract Text:

    jesse d robertsJesse D Roberts,jean-daniel chicheJean-Daniel Chiche,emily m kolpaEmily M Kolpa,donald b blochDonald B Bloch,kenneth d blochKenneth D Bloch,jesse d robertsJesse D Roberts,jean-daniel chicheJean-Daniel Chiche,emily m kolpaEmily M Kolpa,donald b blochDonald B Bloch,kenneth d blochKenneth D Bloch,

    Nitric oxide modulates vascular smooth muscle cell (SMC) cytoskeletal kinetics and phenotype, in part, by stimulating cGMP-dependent protein kinase I (PKGI). To identify molecular targets of PKGI, an interaction trap screen in yeast was performed using a cDNA encoding the catalytic region of PKGI and a human lung cDNA library. We identified a cDNA that encodes a putative PKGI-interactor that is a novel variant of TRIM39, a member of the really interesting new gene (RING) finger family of proteins. Although this TRIM39 variant encodes the NH(2)-terminal RING finger (RF), B-box, and coiled-coil (RBBC) domains of TRIM39, instead of a complete COOH-terminal B30.2 domain, this TRIM39 isoform contains the COOH-terminal portion of Rpp21, a component of RNase P. RT-PCR demonstrated that the TRIM39 variant, which we refer to as TRIM39R, is transcribed in the human fetal lung and in rat pulmonary artery SMC. Indirect immunofluorescence using an antibody generated against the conserved domains of TRIM39 and TRIM39R revealed the proteins in speckled intranuclear structures in human acute monocytic leukemia (THP-1) and human epidermal carcinoma line (HEp-2) cells. PKGI phosphorylated a typical PKGI/PKA phosphorylation domain in a conserved region of TRIM39 and TRIM39R. Additional studies demonstrated that PKGI interacts with both isoforms of TRIM39 in yeast cells and phosphorylates both isoforms of TRIM39 in human cell lines. Although PKGI has been observed to interact with proteins that regulate cytoskeletal function and gene expression, this investigation shows for the first time that PKGI interacts with tripartite motif (TRIM) proteins, which, through diverse molecular pathways, are often observed to regulate important aspects of cellular homeostasis.

    cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Publishing Authors By Initials

    jd robertsJD Roberts,jd chicheJD Chiche,em kolpaEM Kolpa,db blochDB Bloch,kd blochKD Bloch,jd robertsJD Roberts,jd chicheJD Chiche,em kolpaEM Kolpa,db blochDB Bloch,kd blochKD Bloch,

    For similar fungi: yeasts research abstracts see: fungi: yeasts research

    PUBMED ID PMID:

    MEDLINE DATE:

    cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: American journal of physiology. Lung cellular and

    VOLUME: 293

    Page Numbers: L903-12

    Journal Abbreviation: Am. J. Physiol. Lung Cell Mol.

    ISSN: 1040-0605

    DAY: 29

    MONTH: 06

    YEAR: 2007

    cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 100901229

    cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Keywords Mesh Terms:

    KEYWORDS: Yeasts

    MESH TERMS: genetics

    Chemical & Substance for Abstract: cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. Information

    Substance Name: cGMP-dependent protein kinase Ialpha

    Registry Number: EC 2.7.10.-

    Grant and Affiliation Information for cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein.

    AFFILIATION: Department of Anesthesia, Boston, Massachusetts, USA. roberts@cvrc.mgh.harvard.edu

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NHLBI

    GRANT: HL-74352

    ACRONYM: HL

    MEDLINETA: Am J Physiol Lung Cell Mol Phy

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER: EU012025

    Number Hits: 0

    cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein Related Publications

     

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