Comment on “FBXO38 is dispensable for PD-1 regulation” by Dibus et al, [Image: see text]
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Publisher Correction: Cytoplasmic FBXO38 mediates PD-1 degradation.
EMBO Rep
December 2024
CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China.
[Image: see text]
View Article and Find Full Text PDFCytoplasmic FBXO38 mediates PD-1 degradation.
EMBO Rep
October 2024
CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China.
Comment on “FBXO38 is dispensable for PD-1 regulation” by Dibus et al, [Image: see text]
View Article and Find Full Text PDFFBXO38 deficiency promotes lysosome-dependent STING degradation and inhibits cGAS-STING pathway activation.
Neoplasia
March 2024
Department of Ophthalmology, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China; Shanghai Key Laboratory of Orbital Diseases and Ocular Oncology, Shanghai 200025, China. Electronic address:
F-box only protein 38 (FBXO38) is a member of the F-box family that mediates the ubiquitination and proteasome degradation of programmed death 1 (PD-1), and thus has important effects on T cell-related immunity. While its powerful role in adaptive immunity has attracted much attention, its regulatory roles in innate immune pathways remain unknown. The cyclic GMP-AMP synthase-stimulator of interferon genes (cGAS-STING) pathway is an important innate immune pathway that regulates type I interferons.
View Article and Find Full Text PDFMultiple pathways regulate intracellular shuttling of MoKA, a co-activator of transcription factor KLF7.
Nucleic Acids Res
December 2006
Child Health Institute of New Jersey, Robert W. Johnson Medical School, 89 French Street, New Brunswick, NJ 08901, USA.
MoKA is a novel F-box containing protein that interacts with and stimulates the activity of transcription factor KLF7, a regulator of neuronal differentiation. MoKA accumulates throughout the cell and predominantly in the cytosol, consistent with the presence of several putative nuclear localization and export signals (NLSs and NESs). The present study was designed to refine the identity and location of the sequences responsible for MoKA intracellular shuttling and transcriptional activity.
View Article and Find Full Text PDFIdentification of MoKA, a novel F-box protein that modulates Krüppel-like transcription factor 7 activity.
Mol Cell Biol
February 2004
Laboratory of Genetics and Organogenesis, Hospital for Special Surgery at the Weill Medical College of Cornell University, New York, New York 10021, USA.
KLF7, a member of the Krüppel-like transcription factor family, is believed to regulate neurogenesis and cell cycle progression. Here, a yeast two-hybrid screen for KLF7 cofactors in the developing nervous system identified a novel 140-kDa protein named MoKA, for modulator of KLF7 activity. Interaction between MoKA and KLF7 was confirmed by the in vitro glutathione S-transferase pull-down assay and by coimmunoprecipitation of the proteins overexpressed in mammalian cells.
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