Human cytidine triphosphate synthetase 1 interacting proteins.

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Higgins, MJ; Loiselle, D; Haystead, TA; Graves, LM

Published Date

  • June 2008

Published In

Volume / Issue

  • 27 / 6

Start / End Page

  • 850 - 857

PubMed ID

  • 18600551

Electronic International Standard Serial Number (EISSN)

  • 1532-2335

Digital Object Identifier (DOI)

  • 10.1080/15257770802146502

Language

  • eng

Conference Location

  • United States