Abstract
The p24 transmembrane proteins, also known as EMP24/GP25 (endomembrane protein precursor of 24kD (Schimmoller et al., 1995))
proteins, are components of coat protein (COP)-coated vesicles and are present in species as diverse as fungi, plants, flies, worms, and
mammals, indicating that they have important conserved functions. Genetic, molecular, and biochemical characterization of these proteins and
the loci that encode them has provided insights into their potential cellular roles, including postulated functions in vesicle cargo protein
selection and sorting, COPI and COPII vesicle formation and budding, and quality control of proteins that mature through the secretory
pathway. Recently, the first mutations in a Drosophila melanogaster p24 gene have been isolated and characterized. These alleles produce an
interesting behavioral phenotype in females, affecting their ability to oviposit. This identification and mutant characterization of a p24 locus
in Drosophila will pave the way for a better understanding of cell-type-specific functions and interactions among p24 proteins.