Jc. Knol et al., CLONING OF A MOLLUSCAN G-PROTEIN ALPHA-SUBUNIT OF THE GQ CLASS WHICH IS EXPRESSED DIFFERENTIALLY IN IDENTIFIED NEURONS, European journal of biochemistry, 230(1), 1995, pp. 193-199
Through molecular cloning we have identified a molluscan G protein a s
ubunit which belongs to the G alpha(q) family and is expressed in the
central nervous system (CNS) of the pond snail, Lymnaea stagnalis. The
deduced protein product shares a very high degree of amino acid seque
nce identity with vertebrate and invertebrate G alpha(q)/G alpha(11) s
ubunits (80-82% and 76-77%, respectively). Large parts of the protein
have been completely conserved, among which are residues 25-58, includ
ing the nucleotide-binding A domain. Especially the C-terminal half (a
mino acids 195-353), implicated in receptor and effector interactions,
is highly conserved (94% sequence identity with murine sequences). Th
is region includes the nucleotide-binding C, G, and I domains, which a
re identical to cognate motifs of vertebrate G alpha(q/11). Like the l
atter proteins, the Lymnaea G alpha(q) C-terminus lacks a cysteine tha
t could serve as a substrate for pertussis toxin. In situ hybridizatio
n reveals G alpha(q)-encoding mRNA(s) to be present throughout the CNS
. Interestingly, however, close inspection of two identified cell type
s in the cerebral ganglia, the light-green cells, involved in the regu
lation of growth and metabolism and the anterior lobe cells which are
involved in the control of male aspects of reproduction, indicates tha
t they express the mRNA(s) at significantly different levels. Even wit
hin the heterologous cluster of light-green cells there appears to be
differential expression of the pertinent mRNA. Such observations have
hitherto not been reported for specific cell types occurring in vivo.