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URL: https://pubmed.ncbi.nlm.nih.gov/35159164/

⇱ Functional Coordination among the Golgi Complex, the Centrosome and the Microtubule Cytoskeleton during the Cell Cycle - PubMed

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Abstract

The Golgi complex of mammalian cells is organized in a ribbon-like structure often closely associated with the centrosome during interphase. Conversely, the Golgi complex assumes a fragmented and dispersed configuration away from the centrosome during mitosis. The structure of the Golgi complex and the relative position to the centrosome are dynamically regulated by microtubules. Many pieces of evidence reveal that this microtubule-mediated dynamic association between the Golgi complex and centrosome is of functional significance in cell polarization and division. Here, we summarize findings indicating how the Golgi complex and the centrosome cooperate in organizing the microtubule network for the directional protein transport and centrosome positioning required for cell polarization and regulating fundamental cell division processes.

Keywords: Golgi complex; cell migration; centrosome; microtubules; mitosis; mitotic spindle.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

👁 Figure 1
Figure 1
Schematic representation of microtubule polymerization at the Golgi. Microtubule fibres are polymerized starting from the γ-TuRC complex, which is responsible for capping the minus-end microtubules, while microtubules grow in the plus direction. GM130 at the cis-Golgi binds AKAP450, which in turn links CEP215 and MMG to recruit γ-TuRC for nucleation of Golgi-dependent microtubule. After their release from γ-TuRC, the microtubules are stabilized by CAMSAP2 and CLASP1/2, which are connected to the trans-Golgi through GCC185. The interaction between MTCL1 and CLASP1/2 can tether microtubules, whereas the length of the microtubules is regulated by CAMSAP2 when it associates with EBs proteins. The GM130 interactor GRASP65 regulates microtubule stabilization.
👁 Figure 2
Figure 2
Schematic representation of Golgi complex with respect to the centrosome and nucleus. The Golgi complex (GC) is positioned near the centrosome (CE) in front of the nucleus (NU). The cytoskeleton comprises actin (A) and microtubules (MT). Actin controls membrane traffic and rigidity of the Golgi complex, while microtubules can be nucleated both from centrosome (CE) and Golgi (GC). The centrosome regulates the nucleation of a radial array of microtubules (green, MT (GC)) that maintain the pericentriolar localization of the Golgi Complex. The Golgi complex nucleates microtubules (brown, MT (GC)) asymmetrically oriented toward the leading edge. Insets (a,b) represent selected schematic depictions of protein complexes involved in polarized traffic localized at the Golgi complex (a) or at the plasma membrane (b); see the text for more details. Inset (c) shows a selected example of a crucial regulator of post-Golgi traffic, the small GTPases RAB6, which controls protein complexes involved directed secretion to hotspots closely associated with FAs, and that is also transported to FAs through MTs; see the text for more details.
👁 Figure 3
Figure 3
Schematic representation of GC mitotic partitioning and its functional connections with the regulation of mitosis. During the cell cycle, the GC undergoes sequential and reversible disassembly steps. During G2, the Golgi complex is unlinked process thanks to the action of BARS and the phosphorylation of GRASP65 by JNK2 and GRASP55 by ERK1. The G2-specific unlinking is required to activate a Src/Aurora-A mediated pathway to induce centrosome maturation and enter mitosis. After mitosis onset, the Golgi stacks are further disassembled into dispersed vesicles and clusters. Stack disassembly removes a steric hindrance that could hamper spindle formation; the GM130/TPX2/Aurora-A pathway is activated to aid in spindle formation and orientation. In addition, a set of Golgi-structural proteins relocates to the spindle and is repurposed for its proper formation. In turn, the spindle mediates the inheritance of ribbon factors for GC reformation at mitotic exit.
👁 Figure 4
Figure 4
Schematic representation of GRASP65/GM130 complex and its role in polarization and mitosis. GM130 and GRASP65 form a complex at the GC and are involved in cell polarization and cell cycle progression. GM130, composed of six coiled-coil domains, is crucial for microtubules nucleation and spindle assembly and is involved in cell polarization. GRASP65, characterized by two PDZ domains (GRASP domain) and a regulatory domain, controls ribbon organization by multiple mechanisms: tethering of the Golgi stacks, control of microtubules stabilization and local actin polymerization via MENA. The S274 of the regulatory domain is phosphorylated in response to many stimuli, as indicated.

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