Interaction between the PH and START domains of ceramide transfer protein competes with phosphatidylinositol 4-phosphate binding by the PH domain

Samankaltaisia teoksia

• Crystal Structure of the Pleckstrin Homology Domain from the Ceramide Transfer Protein: Implications for Conformational Change upon Ligand Binding
  Tekijä: Prashek, Jennifer, et al.
  Julkaistu: (2013)
• Phosphoinositide binding by the PH domain in ceramide transfer protein (CERT) is inhibited by hyperphosphorylation of an adjacent serine-repeat motif
  Tekijä: Sugiki, Toshihiko, et al.
  Julkaistu: (2018)
• Molecular Basis of Phosphatidylinositol 4-Phosphate and ARF1 GTPase Recognition by the FAPP1 Pleckstrin Homology (PH) Domain
  Tekijä: He, Ju, et al.
  Julkaistu: (2011)
• Ceramide-1-Phosphate, in Contrast to Ceramide, Is Not Segregated into Lateral Lipid Domains in Phosphatidylcholine Bilayers
  Tekijä: Morrow, Michael R., et al.
  Julkaistu: (2009)
• The PH domain from the Toxoplasma gondii PH-containing protein-1 (TgPH1) serves as an ectopic reporter of phosphatidylinositol 3-phosphate in mammalian cells
  Tekijä: Chintaluri, Krishna, et al.
  Julkaistu: (2018)