Analysis of hVps34/hVps15 interactions with Rab5 in vivo and in vitro

Methods Enzymol. 2005:403:789-99. doi: 10.1016/S0076-6879(05)03068-5.

Abstract

The hVps34 phosphatidylinositol (PI) 3-kinase plays an important role in the regulation of vesicular trafficking in the endosomal system. hVps34 associates with a myristylated protein kinase, hVps15. The two proteins are targeting to early endosomal membranes by interactions between hVps15 and activated (GTP-bound) Rab5. This leads to the production of the hVps34 product, PI(3)P, in the endosomal membrane, and subsequent recruitment of FYVE and PX domain-containing effector proteins. This chapter describes the analysis of hVps34/hVps15 interactions with Rab5 in tissue culture cells and in vitro.

MeSH terms

  • Endosomal Sorting Complexes Required for Transport
  • Fluorescent Antibody Technique
  • HeLa Cells
  • Humans
  • In Vitro Techniques
  • Phosphatidylinositol 3-Kinases / metabolism*
  • Protein Binding
  • Protein Biosynthesis
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Transcription, Genetic
  • Vacuolar Sorting Protein VPS15
  • rab5 GTP-Binding Proteins / metabolism

Substances

  • Endosomal Sorting Complexes Required for Transport
  • PIK3R4 protein, human
  • Protein Serine-Threonine Kinases
  • Vacuolar Sorting Protein VPS15
  • rab5 GTP-Binding Proteins