Alternative splicing of CTP:phosphoethanolamine cytidylyltransferase produces two isoforms that differ in catalytic properties.

CTP:phosphoethanolamine cytidylyltransferase (Pcyt2) catalyzes the rate-controlling reaction of the CDP-ethanolamine (Kennedy) pathway. We have previously established that Pcyt2 is encoded by a single gene that can be alternatively spliced from an internal exon into two transcripts, designated Pcyt2alpha and Pcyt2beta. Little is currently known about the regulation of Pcyt2.

Genomic organization, promoter activity, and expression of the human choline transporter-like protein 1.

Choline transporter-like (CTL) proteins of the CTL1 family are novel transmembrane proteins implicated in choline transport for phospholipid synthesis. In this study, we characterized the 5'-flanking region of the human (h)CTL1 gene and examined some of the possible mechanisms of its regulation, including promoter activity, splicing, and expression. The transcription start site of the hCTL1 gene was mapped by 5'-rapid amplification of cDNA ends (RACE), and the presence of two splice variants, hCTL1a and hCTL1b, was investigated using isoform-specific PCR and 3'-RACE.