| First Author | Schnizler MK | Year | 2009 |
| Journal | J Biol Chem | Volume | 284 |
| Issue | 5 | Pages | 2697-705 |
| PubMed ID | 19028690 | Mgi Jnum | J:147232 |
| Mgi Id | MGI:3839719 | Doi | 10.1074/jbc.M805110200 |
| Citation | Schnizler MK, et al. (2009) The cytoskeletal protein alpha-actinin regulates acid-sensing ion channel 1a through a C-terminal interaction. J Biol Chem 284(5):2697-705 |
| abstractText | The acid-sensing ion channel 1a (ASIC1a) is widely expressed in central and peripheral neurons where it generates transient cation currents when extracellular pH falls. ASIC1a confers pH-dependent modulation on postsynaptic dendritic spines and has critical effects in neurological diseases associated with a reduced pH. However, knowledge of the proteins that interact with ASIC1a and influence its function is limited. Here, we show that alpha-actinin, which links membrane proteins to the actin cytoskeleton, associates with ASIC1a in brain and in cultured cells. The interaction depended on an alpha-actinin-binding site in the ASIC1a C terminus that was specific for ASIC1a versus other ASICs and for alpha-actinin-1 and -4. Co-expressing alpha-actinin-4 altered ASIC1a current density, pH sensitivity, desensitization rate, and recovery from desensitization. Moreover, reducing alpha-actinin expression altered acid-activated currents in hippocampal neurons. These findings suggest that alpha-actinins may link ASIC1a to a macromolecular complex in the postsynaptic membrane where it regulates ASIC1a activity. |
