Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
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Drug
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Target Concepts:
Gene/Protein
Disease
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Query: EC:3.1.26.5 (
RNase P
)
1,348
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
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.
...
PMID:cGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein. 1760 97