Questions have been raised about the genomic complexity of the human genome, since it was reported that it only consisted of 32,000 genes. Alternative splicing is considered the explanation of the enormous difference between the number of genes and the number of proteins. Aligning expressed sequence tags (ESTs) to the genomic sequence has become a popular approach for gene prediction, revealing alternative splice variants. The aim in this thesis is to identify and analyse splice variants of the adhesion family of G protein-coupled receptors using EST data. 75% of the genes in the data set of 33 sequences were found to have a total of 51 splice variants. About half of the variants were considered functional.

<p>Questions have been raised about the genomic complexity of the human genome, since it was reported that it only consisted of 32,000 genes. Alternative splicing is considered the explanation of the enormous difference between the number of genes and the number of proteins. Aligning expressed sequence tags (ESTs) to the genomic sequence has become a popular approach for gene prediction, revealing alternative splice variants. The aim in this thesis is to identify and analyse splice variants of the adhesion family of G protein-coupled receptors using EST data. 75% of the genes in the data set of 33 sequences were found to have a total of 51 splice variants. About half of the variants were considered functional.</p>

G proteins coupled receptors (GPCRs) play essential developmental roles with functions in all of the immune, olfactory sensory systems amongst other systems as well as exhibiting essential roles in the central and peripheral nervous system. GPCRs are also major targets of pharmaceutical drugs currently used to treat a vast number of conditions. Despite their clear importance, the function of many GPCRs is still obscure. Identifying the physiological role of more GPCRs provides a niche for more drugs to be developed and thus more conditions to be treated. The C.elegans lat-1 gene encodes the latrophilin vertebrate homolog; it is a member of the adhesion GPCR family and is structurally related to the flamingo/CELSR, an essential component of planar cell polarity pathway. This study aims to phenotypically characterise lat-1 mutants in C.elegans to provide insights into the physiological role of this important member of adhesion GPCRs. lat-1 mutants exhibit several morphological defects throughout development and during vulva development. Analysing the embryonic development of such mutants also identified an anterior-posterior polarity defect. The results implicate a second evolutionary conserved subfamily of adhesion GPCRs in the control of tissue polarity and morphogenesis.