Elsevier

Seminars in Cell Biology

Volume 5, Issue 4, August 1994, Pages 263-272
Seminars in Cell Biology

Regular Article
The PACAP receptor: generation by alternative splicing of functional diversity among G protein-coupled receptors in nerve cells

https://doi.org/10.1006/scel.1994.1032Get rights and content

Abstract

Recent molecular characterization of new G protein-coupled receptors (GPCR) draw attention to alternative splicing as a source of structural diversity. After a brief overview of characterized GPCR splice variants, we will describe in more detail the functional properties of the PACAP type I receptor splice variants. Some of these variants are positively coupled to both adenylate cyclase (AC) and phospholipase C (PLC) whereas others do not elicit any stimulation of the PLC or display a qualitatively intermediate phenotype. The PACAP type I receptor is therefore one of the few examples in which alternative splicing is clearly linked to functional diversity.

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    The other two PACAP receptors VPAC1-R and VPAC2-R are primarily coupled with adenylyl cyclase and have similar binding affinities to VIP and PACAP (Sherwood et al., 2000; Dickson and Finlayson, 2009). In mammals, five PAC1-R isoforms have been identified from the insertion of 28 (hip or hop 1 variant) or 27 (hop 2 variant) amino acid cassettes in intracellular loop 3 (IL3) (Spengler et al., 1993; Journot et al., 1994). In teleosts, PACAP receptor genes have been recently identified in fugu Takifugu rubripes (Cardoso et al., 2004), rainbow trout (Maria Lugo et al., 2011) and other species in the order of Cypriniformes including zebrafish Danio rerio (Fradinger et al., 2005), grass carp Ctenopharyngodon idella (Jiang et al., 2008) and sea bream Sparus aurata (Cardoso et al., 2007).

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    Several splice variants of PAC1 receptor, coupled to the activation of both adenylate cyclase and inositol phosphate/phospholipase C systems have been described (Spengler et al. 1993; Journot et al. 1994; Dautzenberg et al. 1999; Daniel et al. 2001; Vaudry et al. 2009). Most of PAC1 isoforms identified in rat result from alternative splicing in the third intracellular loop (IC3) (Spengler et al. 1993; Journot et al. 1994; Vaudry et al. 2009). The splice variants are characterized by the absence or presence of either one (Hip or Hop1 variant) or two (Hip–Hop) cassettes of 28 or 27 (Hop2 variant) amino acids (Spengler et al. 1993; Journot et al. 1994).

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