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Related Experiment Video

Updated: Feb 15, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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An intrinsic lipid-binding interface controls sphingosine kinase 1 function.

Michael J Pulkoski-Gross1,2, Meredith L Jenkins3, Jean-Philip Truman2

  • 1Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11790.

Journal of Lipid Research
|January 13, 2018
PubMed
Summary
This summary is machine-generated.

Sphingosine kinase 1 (SK1) binds cell membranes via a composite interface, which is crucial for its function in regulating cellular processes like growth and inflammation. This finding offers new therapeutic strategies targeting SK1 in diseases.

Keywords:
cell signalingenzyme regulationhydrogen-deuterium exchange mass spectrometrysphingolipidssphingosine-1-phosphate

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Mechanisms

Background:

  • Sphingosine kinase 1 (SK1) produces sphingosine-1-phosphate (S1P), regulating cellular growth, immune cell trafficking, and inflammation.
  • SK1 requires direct membrane access to sphingosine for S1P production, but the interaction mechanisms are poorly understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms of SK1's direct membrane interactions.
  • To investigate the functional significance of the SK1 membrane-binding interface.

Main Methods:

  • Hydrogen/deuterium exchange mass spectrometry (HDX-MS) to study SK1-membrane vesicle interactions.
  • CRISPR/Cas9 gene editing to generate SK1-deficient HCT116 cells.
  • Analysis of membrane association, SK1 activity, and SK1-dependent signaling pathways.

Main Results:

  • Disruption of the SK1 membrane interface reduced membrane association and cellular SK1 activity.
  • Mutation of the membrane-binding interface abolished SK1-dependent signaling, including cell invasion and endocytosis.
  • A composite interface, comprising electrostatic and hydrophobic sites interacting with anionic phospholipids, was identified as critical for membrane binding.

Conclusions:

  • A composite domain in SK1 governs its membrane-binding ability, which is essential for its cellular functions.
  • Understanding this membrane interaction provides a novel basis for targeting SK1 in disease treatment.