| Title : The conserved RIC-3 coiled-coil domain mediates receptor-specific interactions with nicotinic acetylcholine receptors - Biala_2009_Mol.Biol.Cell_20_1419 |
| Author(s) : Biala Y , Liewald JF , Ben-Ami HC , Gottschalk A , Treinin M |
| Ref : Mol Biology of the cell , 20 :1419 , 2009 |
| Abstract : RIC-3 belongs to a conserved family of proteins influencing nicotinic acetylcholine receptor (nAChR) maturation. RIC-3 proteins are integral membrane proteins residing in the endoplasmic reticulum (ER), and containing a C-terminal coiled-coil domain (CC-I). Conservation of CC-I in all RIC-3 family members indicates its importance; however, previous studies could not show its function. To examine the role of CC-I, we studied effects of its deletion on Caenorhabditis elegans nAChRs in vivo. Presence of CC-I promoted maturation of particular nAChRs expressed in body-wall muscle, whereas it was not required for other nAChR subtypes expressed in neurons or pharyngeal muscles. This effect is receptor-specific, because it could be reproduced after heterologous expression. Consistently, coimmunoprecipitation analysis showed that CC-I enhances the interaction of RIC-3 with a nAChR that requires CC-I in vivo; thus CC-I appears to enhance affinity of RIC-3 to specific nAChRs. However, we found that this function of CC-I is redundant with functions of sequences downstream to CC-I, potentially a second coiled-coil. Alternative splicing in both vertebrates and invertebrates generates RIC-3 transcripts that lack the entire C-terminus, or only CC-I. Thus, our results suggest that RIC-3 alternative splicing enables subtype specific regulation of nAChR maturation. |
| ESTHER : Biala_2009_Mol.Biol.Cell_20_1419 |
| PubMedSearch : Biala_2009_Mol.Biol.Cell_20_1419 |
| PubMedID: 19116311 |
Biala Y, Liewald JF, Ben-Ami HC, Gottschalk A, Treinin M (2009)
The conserved RIC-3 coiled-coil domain mediates receptor-specific interactions with nicotinic acetylcholine receptors
Mol Biology of the cell
20 :1419
Biala Y, Liewald JF, Ben-Ami HC, Gottschalk A, Treinin M (2009)
Mol Biology of the cell
20 :1419