Vesicle fusion, protein import and proteolytic cleavage in eukaryotes
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This publication presents the work from a research dissertation that provided major contributions to the current understanding of intracellular protein trafficking in two important areas: vesicular fusion and peroxisome biogenesis. This effort began with a study of SNAREs, highly conserved proteins that form the core fusion machinery within secretory and endosomal trafficking systems, describing early findings concerning the regulation of an integral member of this protein machinery, syntaxin 5, through its mammalian endoplasmic reticulum/Golgi Sec1/Munc18 protein binding partner rSly1. This r...
This publication presents the work from a research dissertation that provided major contributions to the current understanding of intracellular protein trafficking in two important areas: vesicular fusion and peroxisome biogenesis. This effort began with a study of SNAREs, highly conserved proteins that form the core fusion machinery within secretory and endosomal trafficking systems, describing early findings concerning the regulation of an integral member of this protein machinery, syntaxin 5, through its mammalian endoplasmic reticulum/Golgi Sec1/Munc18 protein binding partner rSly1. This research continued with an examination of peroxisome matrix protein import, a mode of protein transport that utilizes two distinct peroxisomal targeting signals (PTS1 and 2). These studies specifically focused on identifying the PTS2 processing protease. Moreover, two Arabidopsis thaliana proteins possessing both putative PTS1 and and PTS2 signals were examined. Thus, using cellular and molecular biological techniques, this research has expanded the area of intracellular protein trafficking.
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