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J Biol Chem, Vol. 274, Issue 38, 26992-27001, September 17, 1999
SPLICE VARIANT
,, and¶
From the CTP:phosphocholine cytidylyltransferase is a
major regulator of phosphatidylcholine biosynthesis. A single isoform,
CCT Department of Biochemistry, St. Jude
Children's Research Hospital, Memphis, Tennessee 38105 and the
¶ Department of Biochemistry, University of Tennessee,
Memphis, Tennessee 38163
, has been studied extensively and a second isoform, CCT, was
recently identified. We identify and characterize a third cDNA,
CCT2, that differs from CCT1 at the carboxyl-terminal end and is
predicted to arise as a splice variant of the CCT gene. Like CCT,
CCT2 is heavily phosphorylated in vivo, in contrast to
CCT1. CCT1 and CCT2 mRNAs were differentially expressed by
the human tissues examined, whereas CCT was more uniformly
represented. Using isoform-specific antibodies, both CCT1 and
CCT2 localized to the endoplasmic reticulum of cells, in contrast to
CCT which resided in the nucleus in addition to associating with the
endoplasmic reticulum. CCT2 protein has enzymatic activity in
vitro and was able to complement the temperature-sensitive
cytidylyltransferase defect in CHO58 cells, just as CCT and CCT1
supporting proliferation at the nonpermissive conditions.
Overexpression experiments did not reveal discrete physiological
functions for the three isoforms that catalyze the same biochemical
reaction; however, the differential cellular localization and
tissue-specific distribution suggest that CCT1 and CCT2 may play
a role that is distinct from ubiquitously expressed CCT.
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