Checkpoints for vesicular traffic?

Biochem Cell Biol. 2001;79(5):579-85.

Abstract

During interphase the transport of material between different intracellular organelles requires accurate regulation of fusiogenic domains. Recent studies on hepatic endosomes indicated that compartmentalized Cdk2-cyclin E complexes act by braking fusion events. These Cdk2 complexes integrate tyrosine phosphorylation and dephosphorylation inputs, resulting in the control of the number of rounds of fusion at discrete domains. This leads to changes in the intracellular location of internalized receptors and ultimately their biological response.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • CDC2-CDC28 Kinases*
  • Cyclin E / metabolism*
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases / metabolism*
  • DNA / metabolism
  • Endosomes / metabolism
  • Guanosine Triphosphate / metabolism
  • Interphase
  • Ligands
  • Mitosis
  • Models, Biological
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Structure, Tertiary
  • Protein Transport*
  • Protein-Tyrosine Kinases / metabolism
  • Signal Transduction
  • Tyrosine / metabolism

Substances

  • Cyclin E
  • Ligands
  • Tyrosine
  • Guanosine Triphosphate
  • DNA
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • CDC2-CDC28 Kinases
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases