William B. Snyder

TL;DR: This study characterizes ESCRT-II, a soluble approximately 155 kDa protein complex formed by the class E Vps proteins Vps22, Vps25, and Vps36, and proposes that the ESCRT complexes perform a coordinated cascade of events to select and sort MVB cargoes for delivery to the lumen of the vacuole/lysosome.

TL;DR: The principal areas of progress are the identification of new peroxins, definition of protein-protein interactions among peroxin leading to the recognition of complexes involved in peroxisomal protein import, insight into the biogenesis ofperoxisome membrane proteins, and, of most importance, the elucidation of the role of many conservedperoxins in human disease.

TL;DR: The cloned PEX15 encodes a phosphorylated, integral peroxisomal membrane protein (Pex15p), which was found to be a tail‐anchored type II (Ncyt–Clumen) perox IS membrane protein with a single transmembrane domain near its carboxy‐terminus.

TL;DR: The data demonstrate that the amino‐terminal 16 amino acid portion of the ALP cytoplasmic tail domain contains a vacuolar sorting signal which is responsible for the active recognition, packaging and transport of ALP from the Golgi to the vacuole via a novel delivery pathway.

TL;DR: Roles for Pex3p are discussed in the assembly of specific peroxisomal membrane protein subcomplexes whose formation is necessary for matrix protein import.