Calcium sensitivity of α-actinin is required for equatorial actin assembly during cytokinesis

Jayadev, Ranjay; Kuk, Alvin C. Y.; Low, Shyan Huey; Murata‐Hori, Maki

doi:10.4161/cc.20277

Cited by 12 publications

(11 citation statements)

References 41 publications

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“…Multiple actin-binding proteins that mediate actin crosslinking, capping and severing contain Ca 2+ -binding sites (Glenney et al 1987; Jayadev et al 2012). Calcium can also activate other proteins, including calpains, calmodulin, CaMKII and PKC to regulate migration via focal adhesion turnover and cytoskeletal remodeling (Bouvard and Block 1998; Holinstat et al 2003; Lawson and Maxfield 1995).…”

Section: Introductionmentioning

confidence: 99%

“…A key regulator of cytoskeletal reorganization and cell motility is Ca 21 , which mediates downstream signaling cascades that contribute to actin remodeling, retraction of the trailing edge and turnover of adhesion molecules (Wei et al, 2012). Multiple actin-binding proteins that mediate actin crosslinking, capping and severing contain Ca 21 -binding sites (Glenney et al, 1987;Jayadev et al, 2012). Calcium can also activate other proteins, including calpains, calmodulin, CaM-KII and PKC to regulate migration via focal adhesion turnover and cytoskeletal remodeling (Bouvard and Block, 1998;Holinstat et al, 2003;Lawson and Maxfield, 1995).…”

Section: Introductionmentioning

confidence: 99%

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Activation of the TRPV1 cation channel contributes to stress‐induced astrocyte migration

Lambert

Calkins

2014

Glia

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Astrocytes provide metabolic, structural and synaptic support to neurons in normal physiology and also contribute widely to pathogenic processes in response to stress or injury. Reactive astrocytes can undergo cytoskeletal reorganization and increase migration through changes in intracellular Ca2+ mediated by a variety of potential modulators. Here we tested whether migration of isolated retinal astrocytes following mechanical injury (scratch wound) involves the transient receptor potential vanilloid-1 channel (TRPV1), which contributes to Ca2+-mediated cytoskeletal rearrangement and migration in other systems. Application of the TRPV1-specific antagonists, capsazepine (CPZ) or 5’-iodoresiniferatoxin (IRTX), slowed migration by as much as 44%, depending on concentration. In contrast, treatment with the TRPV1-specific agonists, capsaicin (CAP) or resiniferatoxin (RTX) produced only a slight acceleration over a range of concentrations. Chelation of extracellular Ca2+ with EGTA (1 mM) slowed astrocyte migration by 35%. Ratiometric imaging indicated that scratch wound induced a sharp 20% rise in astrocyte Ca2+ that dissipated with distance from the wound. Treatment with IRTX both slowed and dramatically reduced the scratch-induced Ca2+ increase. Both CPZ and IRTX influenced astrocyte cytoskeletal organization, especially near the wound edge. Taken together, our results indicate that astrocyte mobilization in response to mechanical stress involves influx of extracellular Ca2+ and cytoskeletal changes in part mediated by TRPV1 activation.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Activation of the TRPV1 cation channel contributes to stress‐induced astrocyte migration

Lambert

Calkins

2014

Glia

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“…The spatial and temporal regulatory mechanisms underlying the localization of Ain1 have not yet been elucidated. In mammalian cells, the actin-binding activity of α-actinin decreases with Ca 2+ , and Ca 2+ sensitivity is required for the accumulation of α-actinin in the cleavage furrow (52). In contrast, the results of our in vitro experiment indicated that Ca 2+ does not inhibit the actin-bundling activity of Ain1 (Fig.…”

Section: Mechanism Of the Cr-specific Localization Of Ain1mentioning

confidence: 56%

Molecular dissection of the actin-binding ability of the fission yeast α-actinin, Ain1, in vitro and in vivo

Morita

Takaine

Numata

et al. 2017

The Journal of Biochemistry

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A contractile ring (CR) is involved in cytokinesis in animal and yeast cells. Although several types of actin-bundling proteins associate with F-actin in the CR, their individual roles in the CR have not yet been elucidated in detail. Ain1 is the sole α-actinin homologue in the fission yeast Schizosaccharomyces pombe and specifically localizes to the CR with a high turnover rate. S. pombe cells lacking the ain1+ gene show defects in cytokinesis under stress conditions. We herein investigated the biochemical activity and cellular localization mechanisms of Ain1. Ain1 showed weaker affinity to F-actin in vitro than other actin-bundling proteins in S. pombe. We identified a mutation that presumably loosened the interaction between two calponin-homology domains constituting the single actin-binding domain (ABD) of Ain1, which strengthened the actin-binding activity of Ain1. This mutant protein induced a deformation in the ring shape of the CR. Neither a truncated protein consisting only of an N-terminal ABD nor a truncated protein lacking a C-terminal region containing an EF-hand motif localized to the CR, whereas the latter was involved in the bundling of F-actin in vitro. We herein propose detailed mechanisms for how each part of the molecule is involved in the proper cellular localization and function of Ain1.

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“…α‐actinin has been suggested to cross‐link actin under low calcium conditions. However, when intracellular calcium rises (as in the case of a calcium wave), α‐actinin releases actin filaments, thus no longer cross‐linking the F‐actin filaments (Jayadev, Kuk, Low, & Murata‐Hori, ; Prebil et al, ; Sjöblom, Salmazo, & Djinović‐Carugo, ). However, further work will be required to establish the exact connections between calcium and actin networks (Veksler & Gov, ).…”

Section: Discussionmentioning

confidence: 99%

A calcium‐mediated actin redistribution at egg activation in Drosophila

York-Andersen

Wood

et al. 2019

Molecular Reproduction Devel

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Egg activation is the essential process in which mature oocytes gain the competency to proceed into embryonic development. Many events of egg activation are conserved, including an initial rise of intracellular calcium. In some species, such as echinoderms and mammals, changes in the actin cytoskeleton occur around the time of fertilization and egg activation. However, the interplay between calcium and actin during egg activation remains unclear. Here, we use imaging, genetics, pharmacological treatment, and physical manipulation to elucidate the relationship between calcium and actin in living Drosophila eggs. We show that, before egg activation, actin is smoothly distributed between ridges in the cortex of the dehydrated mature oocytes. At the onset of egg activation, we observe actin spreading out as the egg swells though the intake of fluid. We show that a relaxed actin cytoskeleton is required for the intracellular rise of calcium to initiate and propagate. Once the swelling is complete and the calcium wave is traversing the egg, it leads to a reorganization of actin in a wavelike manner. After the calcium wave, the actin cytoskeleton has an even distribution of foci at the cortex. Together, our data show that calcium resets the actin cytoskeleton at egg activation, a model that we propose to be likely conserved in other species.

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Calcium sensitivity of α-actinin is required for equatorial actin assembly during cytokinesis

Cited by 12 publications

References 41 publications

Activation of the TRPV1 cation channel contributes to stress‐induced astrocyte migration

Activation of the TRPV1 cation channel contributes to stress‐induced astrocyte migration

Molecular dissection of the actin-binding ability of the fission yeast α-actinin, Ain1, in vitro and in vivo

A calcium‐mediated actin redistribution at egg activation in Drosophila

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