Main author: Þengill Fannar Jónsson
Institution or Company: Háskóli Íslands
Co-Authors, Institution or Company:
Margrét Helga Ögmundsdóttir, Háskóli Íslands.
Introduction: Autophagy is a conserved degradation process present in all eukaryotic cells. It is necessary for turnover of cellular components to maintain normal homeostasis of the cell.
During autophagy, a double membrane layer termed the phagophore extends from cellular lipid bodies and becomes saturated with cargo, tagged or untagged for degradation. The phagophore proceeds to form a double membrane vesicle, called the autophagosome, in which the autophagic cargo is ultimately degraded. The degraded cargo is repurposed by the cell for other useful components.
A variety of genes regulate and drive autophagy, one of which is GABARAP. GABARAP is one of seven members of the LC3/GABARAP family that all serve similar functions in autophagy. They mainly recognize and recruit other autophagy related proteins to the phagophore, as well as ubiquitinated cargo. Notably, GABARAP has been shown to be involved in more diverse functions.
Methods: In our study we used the TARGET, TCGA, and GTEx mRNA databases for an isoform specific analysis of 66 autophagy related genes.
Results: We identified proportionately high expression levels of two protein coding GABARAP isoforms, alternative to the characterized protein isoform.
Conclusions: The predicted products of the alternative isoforms would lack sections necessary for normal GABARAP function in autophagy. Considering the various roles of GABARAP and the contrast of isoform expression it will be important to determine whether the isoforms are stable as proteins and if so what role/roles they might have. Better understanding of the autophagy machinery is fundamental in furthering our understanding of its role in health and disease.
