Molecular characterization of the organelle contact facilitating protein Pex30 and its role in peroxisome dynamics in Saccharomyces cerevisiae
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Peroxisomes are single membrane-bound organelles found in most eukaryotes. They perform diverse cellular functions depending on the metabolic requirements of the cell. Scavenging harmful reactive oxygen species and β-oxidation of fatty acids are the most well-characterized functions of peroxisomes. They are dynamic in nature whose number and function may vary according to the need of the cell. Peroxisomes interact with other surrounding organelles like mitochondria, lipid droplets, endoplasmic reticulum, etc to optimize their multiple cellular functions. Several peroxisomal proteins have been identified with a role in various facets of peroxisome biogenesis and functions. Pex30 is one such peroxisomal protein that resides in the endoplasmic reticulum and associates with peroxisomes to regulate their biogenesis. It is a 58 kDa protein that consists of an N-terminal reticulon homology domain and an uncharacterized C-terminal dysferlin domain. Recent studies have elucidated the role of Pex30 in the formation of pre-peroxisomal vesicles and lipid droplets from the endoplasmic reticulum. Interestingly, it also associates with the ER reticulon proteins and functions in the maintenance of endoplasmic reticulum morphology.
Supervisors: Nagotu, Shrisha and Thummer, Rajkumar P
Peroxisomes, Phosphorylation, ER, Pex30, Mass Spectrometry, Domain, Dysferlin, Yeast