WIPI2B links PtdIns3P to LC3 lipidation through binding ATG16L1

Autophagy. 2015;11(1):190-1. doi: 10.1080/15548627.2014.996029.


WIPI proteins, phosphatidylinositol 3-phosphate (PtdIns3P) binding proteins with β-propeller folds, are recruited to the omegasome following PtdIns3P production. The functions of the WIPI proteins in autophagosome formation are poorly understood. In a recent study, we reported that WIPI2B directly binds ATG16L1 and functions by recruiting the ATG12-ATG5-ATG16L1 complex to forming autophagosomes during starvation- or pathogen-induced autophagy. Our model of WIPI2 function provides an explanation for the PtdIns3P-dependent recruitment of the ATG12-ATG5-ATG16L1 complex during initiation of autophagy.

Keywords: ATG12–ATG5-ATG16L1; PtdIns3P; PtdIns3P, phosphatidylinositol 3-phosphate; WIPI; autophagosome; autophagy; omegasome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Autophagy
  • Carrier Proteins / metabolism*
  • HeLa Cells
  • Humans
  • Lipids / chemistry*
  • Membrane Proteins / metabolism*
  • Mice
  • Microtubule-Associated Proteins / metabolism*
  • Models, Biological
  • Phosphatidylinositol Phosphates / metabolism*
  • Protein Binding


  • Carrier Proteins
  • Lipids
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Phosphatidylinositol Phosphates
  • phosphatidylinositol 3-phosphate