Human cytidine triphosphate synthetase 1 interacting proteins.
We investigated the interacting proteins and intracellular localization of CTP synthetase 1 (CTPS1) in mammalian cells. CTPS1 interacted with a GST- peptidyl prolyl isomerase, Pin1 fusion (GST-Pin1) in a Ser 575 (S575) phosphorylation-dependent manner. Immunoprecipitation experiments demonstrated that CTPS1 also bound tubulin, and thirteen additional coimmunoprecipitating proteins were identified by mass spectrometry. Immunolocalization experiments showed that tubulin and CTPS1 colocalized subcellularly. Taxol treatment enhanced this but cotreatment of cells with the CTPS inhibitor, cyclopentenyl cytosine (CPEC), and taxol failed to disrupt the colocalization. Thus, these studies provide novel information on the potential interacting proteins that may regulate CTPS1 function or intracellular localization.
Higgins
M J
MJ
Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7365, USA.
Loiselle
D
D
Haystead
T A
TA
Graves
L M
LM
D019731:Carbon-Nitrogen Ligases / Q000276:immunology / Q000378:metabolism*; D002460:Cell Line; D006801:Humans; D047468:Immunoprecipitation; D013058:Mass Spectrometry; D019696:Peptidylprolyl Isomerase / Q000378:metabolism; D011485:Protein Binding
D019696:Peptidylprolyl Isomerase; D019731:Carbon-Nitrogen Ligases; C019951:CTP synthetase