CAP1-mediated actin cycling via ADF/cofilin proteins is essential for asymmetric division in mouse oocytes

Jin, Zhe‐Long; Jo, Yu-Jin; Namgoong, Suk

doi:10.1242/jcs.222356

Cited by 11 publications

(6 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Srv2/CAP is another highly conserved regulator of actin turnover, acting synergistically with cofilin (Kotila et al, 2019;Shekhar et al, 2019). Accordingly, CAP1 knockdown in mouse oocytes was associated with defects in cytoplasmic F-actin, spindle migration and cytokinesis, however no microvillar outgrowth nor actin cap expansion were reported (Jin et al, 2018). Thus, the multiple actin networks that populate the oocyte may be differentially regulated by cofilin, through the assembly of distinct multi-component machineries.…”

Section: Discussionmentioning

confidence: 99%

Cofilin regulates actin network homeostasis and microvilli length in mouse oocytes

Bourdais

Dehapiot

Halet

2021

Journal of Cell Science

View full text Add to dashboard Cite

How multiple actin networks coexist in a common cytoplasm, while competing for a shared pool of monomers, is still an ongoing question. This is exemplified by meiotic maturation in the mouse oocyte, which relies on the dynamic remodeling of distinct cortical and cytoplasmic F-actin networks. Here we show that the conserved actin-depolymerizing factor cofilin is activated in a switch-like manner at meiosis resumption from prophase arrest. Interfering with cofilin activation during maturation resulted in widespread microvilli elongation, while cytoplasmic F-actin was depleted, leading to defects in spindle migration and polar body extrusion. In contrast, cofilin inactivation in metaphase II-arrested oocytes resulted in a shutdown of F-actin dynamics, along with a dramatic overgrowth of the polarized actin cap. However, inhibition of the Arp2/3 complex to promote actin cap disassembly elicited ectopic microvilli outgrowth in the polarized cortex. These data establish cofilin as a key player in actin network homeostasis in oocytes, and reveal that microvilli can act as a sink for monomers upon disassembly of a competing network.

show abstract

Section: Discussionmentioning

confidence: 99%

Cofilin regulates actin network homeostasis and microvilli length in mouse oocytes

Bourdais

Dehapiot

Halet

2021

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…For the generation of constitutively active Cofilin, the Ser‐3 residue was mutated into an alanine residue to prevent phosphorylation 33 . The corresponding mutated gene was cloned into PCS2 + vectors, 18,34 followed by in vitro transcription and poly(A) tailing performed with an SP6 mMessage mMachine Kit and a Poly(A) Tailing Kit (Thermo Fisher Scientific Waltham, MA, USA).…”

Section: Methodsmentioning

confidence: 99%

“…The activity is negatively regulated by phosphorylation at Ser‐3 by LIM kinase, 13 which is activated by small GTPase Rho and its downstream protein kinase ROCK 14,15 . In addition, changes in pH 16 and other regulatory proteins, such as cyclase‐associated protein 5,17,18 also negatively regulate phosphorylation at Ser‐3.…”

Section: Introductionmentioning

confidence: 99%

AIP1 and Cofilin control the actin dynamics to modulate the asymmetric division and cytokinesis in mouse oocytes

et al. 2020

View full text Add to dashboard Cite

Actin-interacting protein 1 (AIP1), also known as WD repeat-containing protein 1 (WDR1), is ubiquitous in eukaryotic organisms, and it plays critical roles in the dynamic reorganization of the actin cytoskeleton. However, the biological function and mechanism of AIP1 in mammalian oocyte maturation is still largely unclear. In this study, we demonstrated that AIP1 boosts ADF/Cofilin activity in mouse oocytes. AIP1 is primarily distributed around the spindle region during oocyte maturation, and its depletion impairs meiotic spindle migration and asymmetric division. The knockdown of AIP1 resulted in the gathering of a large number of actin-positive patches around the spindle region. This effect was reduced by human AIP1 (hAIP1) or Cofilin (S3A) expression. AIP1 knockdown also reduced the phosphorylation of Cofilin near the spindle, indicating that AIP1 interacts with ADF/Cofilin-decorated actin filaments and enhances filament disassembly. Moreover, the deletion of AIP1 disrupts Cofilin localization in metaphase I (MI) and induces cytokinesis defects in metaphase II (MII). Taken together, our results provide evidence that AIP1 promotes actin dynamics and cytokinesis via Cofilin in the gametes of female mice.

show abstract

“…It is a dynamic process controlled by autophagy-related genes (Atg) to maintain normal cellular homeostasis by removing damaged organelles and proteins. Among the Atg, Beclin 1, which is a main regulator of autophagy and it has a role in the formation of autophagosomes [ 13 ]. After autophagy induction, the cytosolic form of the microtubule-associated protein light chain 3 (LC3)-I is conjugated to form LC3-II as an early autophagy marker [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

Sesamol Alleviates the Cytotoxic Effect of Cyclophosphamide on Normal Human Lung WI-38 Cells via Suppressing RAGE/NF-κB/Autophagy Signaling

El-Emam

2020

Nat. Prod. Bioprospect.

View full text Add to dashboard Cite

Cyclophosphamide (CYL) is a chemotherapeutic medication commonly used in managing various malignancies like breast cancer or leukemia. Though, CYL has been documented to induce lung toxicity. Mechanism of CYL toxicity is through oxidative stress and the release of damage-associated molecular patterns (DAMPs). Sesamol (SES) is a natural antioxidant isolated from Sesamum indicum and its effect against CYL-induced lung toxicity is not studied yet. This study aims to investigate whether SES could prevent any deleterious effects induced by CYL on lung using normal human lung cells, WI-38 cell line, without suppressing its efficacy. Cells were pretreated with SES and/or CYL for 24 h, then cell viability was estimated by MTS and trypan blue assays. The mode of cell death was determined by AO/EB staining. Additionally, caspase-3 level, oxidative stress, and inflammatory markers were evaluated by colorimetric and ELISA techniques. qRT-PCR was performed to evaluate RAGE, NF-κB, and Beclin-1 mRNA-expression. CYL-treated WI-38 cells developed a significantly increased cell death with enhanced oxidative and RAGE/NF-κb/Autophagy signaling, which were all attenuated after pretreatment with SES. Thus, we concluded that SES offered a protective role against CYL-induced lung injury via suppressing oxidative stress and RAGE/NF-κB/Autophagy signaling, which is a natural safe therapeutic option against CYL toxicities. Graphic Abstract

show abstract

CAP1-mediated actin cycling via ADF/cofilin proteins is essential for asymmetric division in mouse oocytes

Cited by 11 publications

References 52 publications

Cofilin regulates actin network homeostasis and microvilli length in mouse oocytes

Cofilin regulates actin network homeostasis and microvilli length in mouse oocytes

AIP1 and Cofilin control the actin dynamics to modulate the asymmetric division and cytokinesis in mouse oocytes

Sesamol Alleviates the Cytotoxic Effect of Cyclophosphamide on Normal Human Lung WI-38 Cells via Suppressing RAGE/NF-κB/Autophagy Signaling

Contact Info

Product

Resources

About