Actin-capping proteins play essential roles in asymmetric division of maturing mouse oocytes

Jo, Yu-Jin; Jang, Woo-In; Namgoong, Suk; Kim, Nam‐Hyung

doi:10.1242/jcs.163576

Cited by 32 publications

(33 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, lipopolysaccharide exposure decreased the protein level of p-MAPK. Microtubules form the bipolar spindle, which aligns the chromosomes on the metaphase plate and segregates them into the two daughter cells [32, 33], and actin filaments are responsible for the spindle movement [34]. As a regulator, MAPK plays a key role in microtubule organization and meiotic spindle assembly [35].…”

Section: Discussionmentioning

confidence: 99%

Effects of lipopolysaccharide on maturation of bovine oocyte in vitro and its possible mechanisms

et al. 2016

View full text Add to dashboard Cite

Lipopolysaccharide disturbs the secretion of gonadotropin, endometrial function and implantation efficiency. However, there is little information regarding the effects of lipopolysaccharide on cyclic ovary activity, especially oocyte maturation. Therefore, we aimed to investigate the effects of lipopolysaccharide on the maturation potential of bovine oocytes. We found that lipopolysaccharide exposure significantly decreased the first polar body extrusion rate and delayed the cell cycle progression. The abnormal spindle rate was significantly increased in lipopolysaccharide treatment group, accompanied by disrupted localization and level of phosphorylated mitogen-activated protein kinase (p-MAPK). Moreover, lipopolysaccharide treatment significantly increased intracellular reactive oxygen species (ROS) levels and the early apoptotic rate in oocytes. The pro-apoptotic caspase-3 and Bax mRNA levels and caspase-3 protein level were significantly increased, whereas the anti-apoptotic Bcl-2 and XIAP transcript abundance were significantly decreased in lipopolysaccharide exposure group. Furthermore, the dimethyl-histone H3 lysine 4 (H3K4me2) level was significantly increased, while the DNA methylation (5-mC) and dimethyl-histone H3 lysine 9 (H3K9me2) levels were markedly decreased in oocytes treated with lipopolysaccharide. In conclusion, lipopolysaccharide exposure inhibits the maturation potential of bovine oocytes by affecting cell cycle, cytoskeletal dynamics, oxidative stress, and epigenetic modifications.

show abstract

Section: Discussionmentioning

confidence: 99%

Effects of lipopolysaccharide on maturation of bovine oocyte in vitro and its possible mechanisms

et al. 2016

View full text Add to dashboard Cite

show abstract

“…169 Both CP and Tmod3 are essential for maintaining cytoplasmic actin mesh levels in growing oocytes. 99 Tmod3 and actin binding at the slow-growing end of actin filaments is shown based on the Tmod-actin complex structure (PDB:4PKI, 4PKH). 170 CP and actin binding on the fast-growing ends of filaments was modeled based on the EM reconstitution of actin with CP 171 and the structure of dynactin complex, 172 which contains CP, Actin-related protein 1 (ARP1), and b actin (PDB:5ADX).…”

Section: Actin Depolymerization Factor/cofilinmentioning

confidence: 99%

“…98 When CP expression is reduced by RNAi or inhibited by overexpression of the CP antagonist CARMIL in mouse oocytes, asymmetric division of oocytes is compromised, and cytoplasmic actin mesh levels are significantly reduced. 99 How can CP affect cytoplasmic actin mesh that has been nucleated by formin-2/spire 10,39 ? Recent biochemical studies show that CP and formins can simultaneously bind to the barbed ends and form a ternary complex called a 'decision-complex' involved in elongation or filament end blocking, 100,101 indicating that CPs regulate formin-mediated actin polymerization.…”

Section: Filament End Capping Proteins and Actin Mesh Controlmentioning

confidence: 99%

“…38 (F) Formin-2 and heterodimeric CP compete against each other at the fast-growing filament end and regulate actin elogation 100,101 Because the length of actin filaments generated by formins is much longer than that of cytoplasmic actin mesh 10,37,101 , some mechanism must regulate the elongation of actin filaments by formin-2. Impairment of CP in mouse oocytes decreases cytoplasmic actin density, 99 suggesting that CP regulates actin mesh.…”

Section: Myosin Motors In Oocyte Maturationmentioning

confidence: 99%

See 1 more Smart Citation

Roles of actin binding proteins in mammalian oocyte maturation and beyond

Namgoong

Kim

2016

Cell Cycle

Self Cite

View full text Add to dashboard Cite

Actin nucleation factors, which promote the formation of new actin filaments, have emerged in the last decade as key regulatory factors controlling asymmetric division in mammalian oocytes. Actin nucleators such as formin-2, spire, and the ARP2/3 complex have been found to be important regulators of actin remodeling during oocyte maturation. Another class of actin-binding proteins including cofilin, tropomyosin, myosin motors, capping proteins, tropomodulin, and Ezrin-Radixin-Moesin proteins are thought to control actin cytoskeleton dynamics at various steps of oocyte maturation. In addition, actin dynamics controlling asymmetric-symmetric transitions after fertilization is a new area of investigation. Taken together, defining the mechanisms by which actin-binding proteins regulate actin cytoskeletons is crucial for understanding the basic biology of mammalian gamete formation and pre-implantation development.

show abstract

“…Rho‐kinase (ROCK) is a major downstream effector of the small GTPase RhoA and promotes actin organization by phosphorylating several downstream target proteins including myosin light chain, LIM kinase, and cofilin during meiotic maturation (17, 19, 20). Besides actin nucleators and small GTPase proteins, the function of other actin binding proteins, including capping proteins (21), tropomodulin (22), and tropomyosins (23) have been emerged in oocytes. These proteins have been shown to be important in the maintenance of cytoplasmic actin mesh network in mouse oocytes.…”

mentioning

confidence: 99%

Filamin A is required for spindle migration and asymmetric division in mouse oocytes

et al. 2017

Self Cite

View full text Add to dashboard Cite

Dynamic changes in the actin network are crucial for the cortical migration of spindles and establishment of polarity, to ensure asymmetric division during meiotic maturation. In this study, filamin A (FLNA) was found to be an essential actin regulator that controlled spindle migration and asymmetric division during oocyte meiosis. FLNA was localized in the cytoplasm and enriched at the cortex and near the chromosomes. Knockdown of FLNA impaired meiotic asymmetric division and spindle migration with a decrease in the amount of cytoplasmic actin mesh and cortical actin levels. Moreover, FLNA knockdown reduced the phosphorylation of cofilin and Rho kinase (ROCK) near the spindle. Similar phenotypes, such as decreased filament actin levels, impaired spindle migration and polar body extrusion, were observed when active cofilin (S3A) was overexpressed or ROCK was inhibited. Notably, we found that FLNA and ROCK interacted directly in mouse oocytes. Taken together, our results show that FLNA plays crucial roles in asymmetric division during meiotic maturation by regulating ROCK-cofilin-mediated actin reorganization.-Wang, H., Guo J., Lin, Z., Namgoong, S., Oh, J. S., Kim, N.-H. Filamin A is required for spindle migration and asymmetric division in mouse oocytes. FASEB J. 31, 3677-3688 (2017

show abstract

Actin-capping proteins play essential roles in asymmetric division of maturing mouse oocytes

Cited by 32 publications

References 62 publications

Effects of lipopolysaccharide on maturation of bovine oocyte in vitro and its possible mechanisms

Effects of lipopolysaccharide on maturation of bovine oocyte in vitro and its possible mechanisms

Roles of actin binding proteins in mammalian oocyte maturation and beyond

Filamin A is required for spindle migration and asymmetric division in mouse oocytes

Contact Info

Product

Resources

About