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.
Duke Scholars
Altmetric Attention Stats
Dimensions Citation Stats
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Protein Binding
- Peptidylprolyl Isomerase
- Organic Chemistry
- Mass Spectrometry
- Immunoprecipitation
- Humans
- Cell Line
- Carbon-Nitrogen Ligases
- 3404 Medicinal and biomolecular chemistry
- 3101 Biochemistry and cell biology
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Protein Binding
- Peptidylprolyl Isomerase
- Organic Chemistry
- Mass Spectrometry
- Immunoprecipitation
- Humans
- Cell Line
- Carbon-Nitrogen Ligases
- 3404 Medicinal and biomolecular chemistry
- 3101 Biochemistry and cell biology