preprints.org > biology and life sciences > cell and developmental biology > doi: 10.20944/preprints202312.0206.v1

Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 4 December 2023 / Approved: 4 December 2023 / Online: 5 December 2023 (04:48:31 CET)

<I>Saccharomyces cerevisiae</I> proliferates by budding, which includes the formation of a cytoplasmic protrusion called the ‘bud’, into which DNA, RNA, proteins, organelles, and other materials are transported. The transport of organelles into the growing bud must be strictly regulated for proper inheritance of organelles by daughter cells. In yeast, E3 ubiquitin ligases are involved in inheritance of mitochondria, vacuoles, and peroxisomes. These organelles are transported toward the tip of the growing bud by the myosin motor protein Myo2 along actin filaments. During organelle transport, adaptor proteins bridge the organelles and myosin. After reaching the bud, the adaptor proteins are ubiquitinated by E3 ubiquitin ligases and then degraded by the proteasome. Targeted degradation of the adaptor proteins is necessary to unload to unload the organelles from the actin–myosin machinery. Impairment of the ubiquitination of adaptor proteins results in a failure of organelle release from myosin, which in turn leads to abnormal dynamics, morphology, and function of the inherited organelles. Here, we summarize the role and regulation of E3 ubiquitin ligases during organelle inheritance in yeast.

ubiquitin; E3 ligase; proteolysis; vacuole; mitochondria; peroxisome; myosin; yeast

Biology and Life Sciences, Cell and Developmental Biology

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