Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.4.2.30 (
PARP
)
13,611
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Mammalian mitochondrial ribosomes synthesize 13 proteins that are essential for oxidative phosphorylation. In addition to their role in protein synthesis, some of the mitochondrial ribosomal proteins have acquired functions in other cellular processes such as apoptosis.
Death-associated protein 3
(
DAP3
), also referred to as
mitochondrial ribosomal protein S29
(
MRP-S29
), is a GTP-binding pro-apoptotic protein located in the small subunit of the ribosome. Previous studies have shown that phosphorylation is one of the most likely regulatory mechanisms for
DAP3
function in apoptosis and may be in protein synthesis; however, no phosphorylation sites were identified. In this study, we have investigated the phosphorylation status of ribosomal
DAP3
and mapped the phosphorylation sites by tandem mass spectrometry. Mitochondrial ribosomal
DAP3
is phosphorylated at Ser215 or Thr216, Ser220, Ser251 or Ser252, and Ser280. In addition, phosphorylation of recombinant
DAP3
by Protein kinase A and Protein kinase Cdelta at residues that are endogenously phosphorylated in ribosomal
DAP3
suggests both of these kinases as potential candidates responsible for the in vivo phosphorylation of
DAP3
in mammalian mitochondria. Interestingly, the majority of the phosphorylation sites detected in our study are clustered around the highly conserved GTP-binding motifs, speculating on the significance of these residues on protein conformation and activity. Site-directed mutagenesis studies on selected phosphorylation sites were performed to determine the effect of phosphorylation on cell proliferation and
PARP
cleavage as indication of caspase activation. Overall, our findings suggest
DAP3
, a mitochondrial ribosomal small subunit protein, is a novel phosphorylated target.
...
PMID:Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3. 1822 31
