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Characterization of a chromatin-associated TCF7L1 complex in human embryonic stem cells.
Vuong, Linh M; Pan, Songqin; Sierra, Robert A; Waterman, Marian L; Gershon, Paul D; Donovan, Peter J.
Affiliation
  • Vuong LM; Department of Developmental and Cell Biology, University of California, Irvine, California, USA.
  • Pan S; Department of Biological Chemistry, University of California, Irvine, California, USA.
  • Sierra RA; Sue and Bill Gross Stem Cell Research Center: A CIRM Institute, University of California, Irvine, California, USA.
  • Waterman ML; W.M. Keck Proteomics Laboratory, Institute of Integrated Genome Biology, Department of Botany and Plant Sciences, University of California, Riverside, California, USA.
  • Gershon PD; Department of Biological Chemistry, University of California, Irvine, California, USA.
  • Donovan PJ; Sue and Bill Gross Stem Cell Research Center: A CIRM Institute, University of California, Irvine, California, USA.
Proteomics ; : e2300641, 2024 Apr 17.
Article in En | MEDLINE | ID: mdl-38629187
ABSTRACT
Human embryonic stem cells (hESCs) resemble the pluripotent epiblast cells found in the early postimplantation human embryo and represent the "primed" state of pluripotency. One factor that helps primed pluripotent cells retain pluripotency and prepare genes for differentiation is the transcription factor TCF7L1, a member of a small family of proteins known as T cell factors/Lymphoid enhancer factors (TCF/LEF) that act as downstream components of the WNT signaling pathway. Transcriptional output of the WNT pathway is regulated, in part, by the activity of TCF/LEFs in conjunction with another component of the WNT pathway, ß-CATENIN. Because TCF7L1 plays an important role in regulating pluripotency, we began to characterize the protein complex associated with TCF7L1 when bound to chromatin in hESCs using rapid immunoprecipitation of endogenous proteins (RIME).  Data are available via ProteomeXchange with identifier PXD047582. These data identify known and new partners of TCF7L1 on chromatin and provide novel insights into how TCF7L1 and pluripotency itself might be regulated.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Proteomics Journal subject: BIOQUIMICA Year: 2024 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Proteomics Journal subject: BIOQUIMICA Year: 2024 Document type: Article Affiliation country: United States
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