PUBLICATION
Amino acid variations resulting in functional and nonfunctional zebrafish P2X(1) and P2X (5.1) receptors
- Authors
- Low, S.E., Kuwada, J.Y., and Hume, R.I.
- ID
- ZDB-PUB-081022-21
- Date
- 2008
- Source
- Purinergic signalling 4(4): 383-392 (Journal)
- Registered Authors
- Kuwada, John, Low, Sean
- Keywords
- Zebrafish, P2X receptors, Skeletal muscle, Myogenesis
- MeSH Terms
- none
- PubMed
- 18850305 Full text @ Purinergic Signal.
Citation
Low, S.E., Kuwada, J.Y., and Hume, R.I. (2008) Amino acid variations resulting in functional and nonfunctional zebrafish P2X(1) and P2X (5.1) receptors. Purinergic signalling. 4(4):383-392.
Abstract
Several zebrafish P2X receptors (zP2X(1), zP2X(2), and zP2X(5.1)) have been reported to produce little or no current although their mammalian orthologs produce functional homomeric receptors. We isolated new cDNA clones for these P2X receptors that revealed sequence variations in each. The new variants of zP2X(1) and zP2X(5.1) produced substantial currents when expressed by Xenopus oocytes, however the new variant of zP2X(2) was still nonfunctional. zP2X(2) lacks two lysine residues essential for ATP responsiveness in other P2X receptors; however introduction of these two lysines was insufficient to allow this receptor to function as a homotrimer. We also tested whether P2X signaling is required for myogenesis or synaptic communication at the zebrafish neuromuscular junction. We found that embryonic skeletal muscle expressed only one P2X receptor, P2X(5.1). Antisense knockdown of P2X(5.1) eliminated skeletal muscle responsiveness to ATP but did not prevent myogenesis or behaviors that require functional transmission at the neuromuscular junction.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping