| First Author | Sánchez-Ponce D | Year | 2012 |
| Journal | Cereb Cortex | Volume | 22 |
| Issue | 7 | Pages | 1648-61 |
| PubMed ID | 21940706 | Mgi Jnum | J:198548 |
| Mgi Id | MGI:5496993 | Doi | 10.1093/cercor/bhr251 |
| Citation | Sanchez-Ponce D, et al. (2012) Colocalization of alpha-actinin and synaptopodin in the pyramidal cell axon initial segment. Cereb Cortex 22(7):1648-61 |
| abstractText | The cisternal organelle that resides in the axon initial segment (AIS) of neocortical and hippocampal pyramidal cells is thought to be involved in regulating the Ca(2+) available to maintain AIS scaffolding proteins, thereby preserving normal AIS structure and function. Through immunocytochemistry and correlative light and electron microscopy, we show here that the actin-binding protein alpha-actinin is present in the typical cistenal organelle of rodent pyramidal neurons as well as in a large structure in the AIS of a subpopulation of layer V pyramidal cells that we have called the "giant saccular organelle." Indeed, this localization of alpha-actinin in the AIS is dependent on the integrity of the actin cytoskeleton. Moreover, in the cisternal organelle of cultured hippocampal neurons, alpha-actinin colocalizes extensively with synaptopodin, a protein that interacts with both actin and alpha-actinin, and they appear concomitantly during the development of these neurons. Together, these results indicate that alpha-actinin and the actin cytoskeleton are important components of the cisternal organelle that are probably required to stabilize the AIS. |
