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 th...

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Bibliographic Details
Published in:Nucleosides, nucleotides & nucleic acids nucleotides & nucleic acids, 2008-06, Vol.27 (6-7), p.850-857
Main Authors: Higgins, M. J., Loiselle, D., Haystead, T. A., Graves, L. M.
Format: Article
Language:English
Subjects:
Carbon-Nitrogen Ligases - immunology
Carbon-Nitrogen Ligases - metabolism
Cell Line
CTP
CTP synthetase
Humans
Immunoprecipitation
localization
Mass Spectrometry
Peptidylprolyl Isomerase - metabolism
Pin1
Protein Binding
tubulin
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Summary: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.
ISSN:1525-7770
1532-2335
DOI:10.1080/15257770802146502