Members of the p24 protein family form a highly conserved family of type I transmembrane proteins that are abundant components of the early secretory pathway. Topologically, the proteins have a large luminal domain and a short cytoplasmic domain that allows for targeting to both coat protein complex II and coat protein complex I vesicles, and thus these proteins cycle between the endoplasmic reticulum and Golgi compartments. Several functions have been proposed for these proteins including a role in coat protein complex I vesicle biogenesis, cargo protein selection, organization of intracellular membranes, and protein quality control. Recent studies have added to the list of potential cargo substrates for which p24 function is required for normal transport in the secretory pathway. This review focuses on recent developments in the study of p24 proteins and their requirement for secretory and membrane protein transport in eukaryotic cells.
About the authors
Irmgard Schuiki, obtained her PhD (Dr.rer.nat) in cell biology in 2008 from the Institute of Biochemistry, Graz University of Technology, Graz, Austria. Her research focused on yeast phospholipid homeostasis. Since 2009 she has been a post-doctoral fellow in the Division of Cellular and Molecular Biology, Toronto General Research Institute, Toronto, Canada. Her research focuses on pancreatic β-cell biology.
Allen Volchuk, obtained his PhD in biochemistry from the Department of Biochemistry, University of Toronto, Canada working on insulin regulated glucose transport in adipose and muscle cells. Following post-doctoral studies at Sloan-Kettering Institute in New York City studying protein transport in the Golgi complex, since 2004 he has been a principle investigator (Scientist) in the Division of Cellular and Molecular Biology, Toronto General Research Institute, focusing on pancreatic β-cell biology in the context of type 2 diabetes.
©2012 by Walter de Gruyter Berlin Boston