Regulation of cell polarity by controlled proteolytic systems

Bórquez, Daniel A.; González-Billault, Christian

doi:10.4067/s0716-97602011000100005

Cited by 6 publications

(6 citation statements)

References 73 publications

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“…In metazoans, the Cys proteases calpains are integral components of the cell polarization machinery (Bórquez and González-Billault, 2011). Being essential for embryogenesis and seed development, plant calpain-like protease Dek1 (for Defective kernel1) has not been implicated in the regulation of cell polarity (Lid et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

The Caspase-Related Protease Separase (EXTRA SPINDLE POLES) Regulates Cell Polarity and Cytokinesis inArabidopsis

et al. 2013

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Vesicle trafficking plays an important role in cell division, establishment of cell polarity, and translation of environmental cues to developmental responses. However, the molecular mechanisms regulating vesicle trafficking remain poorly understood. Here, we report that the evolutionarily conserved caspase-related protease separase (EXTRA SPINDLE POLES [ESP]) is required for the establishment of cell polarity and cytokinesis in Arabidopsis thaliana. At the cellular level, separase colocalizes with microtubules and RabA2a (for RAS GENES FROM RAT BRAINA2a) GTPase-positive structures. Separase facilitates polar targeting of the auxin efflux carrier PIN-FORMED2 (PIN2) to the rootward side of the root cortex cells. Plants with the radially swollen4 (rsw4) allele with compromised separase activity, in addition to mitotic failure, display isotropic cell growth, perturbation of auxin gradient formation, slower gravitropic response in roots, and cytokinetic failure. Measurements of the dynamics of vesicle markers on the cell plate revealed an overall reduction of the delivery rates of KNOLLE and RabA2a GTPase in separase-deficient roots. Furthermore, dissociation of the clathrin light chain, a protein that plays major role in the formation of coated vesicles, was slower in rsw4 than in the control. Our results demonstrate that separase is a key regulator of vesicle trafficking, which is indispensable for cytokinesis and the establishment of cell polarity.

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Section: Discussionmentioning

confidence: 99%

The Caspase-Related Protease Separase (EXTRA SPINDLE POLES) Regulates Cell Polarity and Cytokinesis inArabidopsis

et al. 2013

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“…Localization and activity of polarity proteins is heavily regulated through kinases and phosphatases [10][11][12]. In addition, increasing evidence suggests that protein stability via proteasomal degradation contributes to polarity control [13]. While the regulation of cell polarity at the protein level is fairly well understood, it is less well understood how the expression of genes encoding polarity proteins is regulated.…”

Section: Introductionmentioning

confidence: 99%

Transcriptional Control of Apical-Basal Polarity Regulators

Rust

Wodarz

2021

IJMS

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Cell polarity is essential for many functions of cells and tissues including the initial establishment and subsequent maintenance of epithelial tissues, asymmetric cell division, and morphogenetic movements. Cell polarity along the apical-basal axis is controlled by three protein complexes that interact with and co-regulate each other: The Par-, Crumbs-, and Scrib-complexes. The localization and activity of the components of these complexes is predominantly controlled by protein-protein interactions and protein phosphorylation status. Increasing evidence accumulates that, besides the regulation at the protein level, the precise expression control of polarity determinants contributes substantially to cell polarity regulation. Here we review how gene expression regulation influences processes that depend on the induction, maintenance, or abolishment of cell polarity with a special focus on epithelial to mesenchymal transition and asymmetric stem cell division. We conclude that gene expression control is an important and often neglected mechanism in the control of cell polarity.

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“…The core particle (20S proteasome) requires the regulatory particle (19S) to degrade ubiquitinated protein substrates (20). There are several reports that indicate that the UPS can regulate actin dynamics and control cell polarity (21–23). For instance in neurons, the proteasome is actively depleted from the growth cones in order to increase the accumulation of proteins that trigger cytoskeleton polymerization and thereby promote their extension (24).…”

Section: Introductionmentioning

confidence: 99%

Proteasome Dependent Actin Remodeling Facilitates Antigen Extraction at the Immune Synapse of B Cells

et al. 2019

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Engagement of the B cell receptor (BCR) with surface-tethered antigens leads to the formation of an immune synapse (IS), where cell signaling and antigen uptake are tightly coordinated. Centrosome re-orientation to the immune synapse has emerged as a critical regulatory step to guide the local recruitment and secretion of lysosomes, which can facilitate the extraction of immobilized antigens. This process is coupled to actin remodeling at the centrosome and at the immune synapse, which is crucial to promote cell polarity. How B cells balance both pools of actin cytoskeleton to achieve a polarized phenotype during the formation of an immune synapse is not fully understood. Here, we reveal that B cells rely on proteasome activity to achieve this task. The proteasome is a multi-catalytic protease that degrades cytosolic and nuclear proteins and its dysfunction is associated with diseases, such as cancer and autoimmunity. Our results show that resting B cells contain an active proteasome pool at the centrosome, which is required for efficient actin clearance at this level. As a result of proteasome inhibition, activated B cells do not deplete actin at the centrosome and are unable to separate the centrosome from the nucleus and thus display impaired polarity. Consequently, lysosome recruitment to the immune synapse, antigen extraction and presentation are severely compromised in B cells with diminished proteasome activity. Additionally, we found that proteasome inhibition leads to impaired actin remodeling at the immune synapse, where B cells display defective spreading responses and distribution of key signaling molecules at the synaptic membrane. Overall, our results reveal a new role for the proteasome in regulating the immune synapse of B cells, where the intracellular compartmentalization of proteasome activity controls cytoskeleton remodeling between the centrosome and synapse, with functional repercussions in antigen extraction and presentation.

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Regulation of cell polarity by controlled proteolytic systems

Cited by 6 publications

References 73 publications

The Caspase-Related Protease Separase (EXTRA SPINDLE POLES) Regulates Cell Polarity and Cytokinesis inArabidopsis

The Caspase-Related Protease Separase (EXTRA SPINDLE POLES) Regulates Cell Polarity and Cytokinesis inArabidopsis

Transcriptional Control of Apical-Basal Polarity Regulators

Proteasome Dependent Actin Remodeling Facilitates Antigen Extraction at the Immune Synapse of B Cells

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