Related Experiment Video

Updated: Feb 8, 2026

Mouse Embryonic Development in a Serum-free Whole Embryo Culture System
08:55

Mouse Embryonic Development in a Serum-free Whole Embryo Culture System

Published on: March 1, 2014

26.8K

Involvement of LIMK1/2 in actin assembly during mouse embryo development

Xing Duan1, Hao-Lin Zhang1, Lan-Lan Wu1

  • 1a College of Animal Science and Technology , Nanjing Agricultural University , Nanjing , China.

Cell Cycle (Georgetown, Tex.)
|June 27, 2018
PubMed

LIMKs (LIMK1 and LIMK2) are serine/threonine protein kinases that involve in various cellular activities such as cell migration, morphogenesis and cytokinesis. However, its roles during mammalian early embryo development are still unclear. In the present study, we disrupted LIMK1/2 activity to explore the functions of LIMK1/2 during mouse early embryo development. We found that p-LIMK1/2 mainly located at the cortex of each blastomeres from 2-cell to 8-cell stage, and p-LIMK1/2 also expressed at morula and blastocyst stage in mouse embryos. Inhibition of LIMK1/2 activity by LIMKi 3 (BMS-5) at the zygote stage caused the failure of embryo early cleavage, and the disruption of LIMK1/2 activity at 8-cell stage caused the defects of embryo compaction and blastocyst formation. Fluorescence staining and intensity analysis results demonstrated that the inhibition of LIMK1/2 activity caused aberrant cortex actin expression and the decrease of phosphorylated cofilin in mouse embryos. Taken together, we identified LIMK1/2 as an important regulator for cofilin phosphorylation and actin assembly during mouse early embryo development.

Keywords:
LIMK1/2actinblastocystembryo development

More Related Videos

Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos07:57

Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos

Published on: May 15, 2020

3.9K
Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

3.2K

Related Concept Videos

Piaget's Stage 2 of Cognitive Development01:14

Piaget's Stage 2 of Cognitive Development

The preoperational stage, the second of Jean Piaget's four stages of cognitive development, spans approximately ages 2 to 7 and is characterized by the emergence of symbolic thinking. During this stage, children use language, images, and symbols to represent objects and concepts, enabling them to engage in imaginative and pretend play. This symbolic thinking supports children's ability to perform make-believe actions, such as imagining a broom as a horse or their hand as a phone, blending...
947
Development of the Sexual Organs in the Embryo and Fetus01:15

Development of the Sexual Organs in the Embryo and Fetus

Development of the reproductive organs in an embryo starts from a bipotential state. This means the early embryo can develop either male or female reproductive organs. The formation of these organs begins with the growth of gonadal ridges that arise from the intermediate mesoderm during the fifth week of development.
Near the gonadal ridges, two duct systems are present: the mesonephric ducts (Wolffian ducts) and paramesonephric ducts (Müllerian ducts). These ducts form the basis for the...
3.8K
Actin Treadmilling01:18

Actin Treadmilling

Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
9.7K
Introduction to Actin01:26

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
6.6K
Actin Polymerization01:42

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
8.6K
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.8K