Abstract
Here, we characterize spatial distribution of the Golgi complex in human cells. In contrast to the prevailing view that the Golgi compactly surrounds the centrosome throughout interphase, we observe characteristic differences in the morphology of Golgi ribbons and their association with the centrosome during various periods of the cell cycle. The compact Golgi complex is typical in G1; during S-phase, Golgi ribbons lose their association with the centrosome and extend along the nuclear envelope to largely encircle the nucleus in G2. Interestingly, pre-mitotic separation of duplicated centrosomes always occurs after dissociation from the Golgi. Shortly before the nuclear envelope breakdown, scattered Golgi ribbons reassociate with the separated centrosomes restoring two compact Golgi complexes. Transitions between the compact and distributed Golgi morphologies are microtubule-dependent. However, they occur even in the absence of centrosomes, which implies that Golgi reorganization is not driven by the centrosomal microtubule asters. Cells with different Golgi morphology exhibit distinct differences in the directional persistence and velocity of migration. These data suggest that changes in the radial distribution of the Golgi around the nucleus define the extent of cell polarization and regulate cell motility in a cell cycle-dependent manner.
Highlights
The Golgi complex serves as a major hub for intracellular trafficking, allowing for the proper processing of newly synthesized proteins, their sorting, and transport toward proper destinations.The complex comprises polarized stacks of flattened cisternae, which receive proteins translated within the endoplasmic reticulum (ER) at the cis face
Analysis of the Golgi morphology and its association with the centrosome in fixed cells randomly selected from asynchronous populations of human euploid RPE1 line suggests prominent cell cycle specific differences in the organization of this organelle
Prophase was identified as the period when the condensed chromosomes within the intact nucleus can be morphologically detected (Figure 1a)
Summary
The Golgi complex serves as a major hub for intracellular trafficking, allowing for the proper processing of newly synthesized proteins, their sorting, and transport toward proper destinations.The complex comprises polarized stacks of flattened cisternae, which receive proteins translated within the endoplasmic reticulum (ER) at the cis face. The Golgi complex serves as a major hub for intracellular trafficking, allowing for the proper processing of newly synthesized proteins, their sorting, and transport toward proper destinations. Due to its vital role in protein trafficking, organization of the Golgi has been studied extensively and the consensus is that the localization and morphology of the Golgi are governed by the cytoskeleton. This governance allows for highly dynamic changes in the organization of Golgi that are paramount for the proper function of this organelle. Golgi stacks are linked via tubular connections into a Golgi ribbon whose integrity is important for its role as the central protein processing and sorting station. Fragmentation involves a breakdown of the Golgi ribbon into individual stacks [4], unstacking and vesiculation of
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