PtdIns(3,5)P2 finds a partner.
Phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P(2)) is required for the sorting of a subset of membrane proteins at the late endosome. Unlike other phosphoinositides, binding partners for PtdIns(3,5)P(2) and its mechanism of action have not been characterized. New work by in this issue of Developmental Cell describes the identification of a yeast epsin-like protein that binds PtdIns(3,5)P(2) and functions in the transport of proteins through late endosomes to the lysosome-like vacuole.
Hicke
Linda
L
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
D033942:Adaptor Proteins, Vesicular Transport; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D011992:Endosomes / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D008247:Lysosomes / Q000378:metabolism; D009479:Neuropeptides / Q000378:metabolism*; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000502:physiology; D021381:Protein Transport; D051381:Rats; D014617:Vacuoles / Q000378:metabolism; D033921:Vesicular Transport Proteins; D015003:Yeasts
D033942:Adaptor Proteins, Vesicular Transport; D002352:Carrier Proteins; D005656:Fungal Proteins; D009479:Neuropeptides; D018129:Phosphatidylinositol Phosphates; D033921:Vesicular Transport Proteins; C114154:epsin; C106336:phosphatidylinositol 3,5-diphosphate