evolutionary strata of DARPP-32 tail implicates hierarchical functional expansion in higher vertebrates

DARPP-32 (dopamine and adenosine 3′,5′-monophosphate-regulated phosphoprotein of 32 kDa), which belongs to PPP1R1 gene family, is known to act as an important integrator in dopamine-mediated neurotransmission via the inhibition of protein phosphatase-1 (PP1). Besides its neuronal roles, this protein...

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Bibliographic Details
Published in:Journal of biosciences 2014-06, Vol.39 (3), p.493-504
Main Authors: Ung, Choong Yong, Teoh, Teow Chong
Format: Article
Language:English
Subjects:
adenosine
Amino Acid Sequence
Animals
Binding Sites
Bioinformatics
Biomedical and Life Sciences
Biomedicine
Cell Biology
Computational Biology
Conserved Sequence
dopamine
Dopamine and cAMP-Regulated Phosphoprotein 32 - chemistry
Evolution, Molecular
Evolutionary biology
genes
Humans
Life Sciences
Microbiology
phosphoprotein phosphatase
phosphoproteins
Phosphorylation
Phylogenetics
Phylogeny
Plant Sciences
Proteins
Sequence Alignment
Sequence Analysis, Protein
Synteny
Vertebrates
Zoology
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Summary:DARPP-32 (dopamine and adenosine 3′,5′-monophosphate-regulated phosphoprotein of 32 kDa), which belongs to PPP1R1 gene family, is known to act as an important integrator in dopamine-mediated neurotransmission via the inhibition of protein phosphatase-1 (PP1). Besides its neuronal roles, this protein also behaves as a key player in pathological and pharmacological aspects. Use of bioinformatics and phylogenetics approaches to further characterize the molecular features of DARPP-32 can guide future works. Predicted phosphorylation sites on DARPP-32 show conservation across vertebrates. Phylogenetics analysis indicates evolutionary strata of phosphorylation site acquisition at the C-terminus, suggesting functional expansion of DARPP-32, where more diverse signalling cues may involve in regulating DARPP-32 in inhibiting PP1 activity. Moreover, both phylogenetics and synteny analyses suggest de novo origination of PPP1R1 gene family via chromosomal rearrangement and exonization.
ISSN:0250-5991
0973-7138
DOI:10.1007/s12038-014-9438-8