The small GTPase Arf6 regulates sea urchin morphogenesis
Nadezda A Stepicheva1, Megan Dumas1, Priscilla Kobi1
1Department of Biological Sciences, University of Delaware, Newark, DE 19716, United States.
Differentiation; Research in Biological Diversity
|February 12, 2017
Summary
The small GTPase Arf6 is crucial for embryonic development, influencing cell migration and skeleton formation in sea urchins by remodeling actin and affecting cell adhesion. Its role in cellular morphogenesis highlights its importance in forming embryonic structures.
Area of Science:
- Developmental Biology
- Cell Biology
- Molecular Biology
Background:
- The small GTPase Arf6 is a conserved protein involved in cytoskeletal actin remodeling and membrane trafficking.
- While Arf6's cellular functions are well-studied, its physiological role in embryonic development remains largely unknown.
Purpose of the Study:
- To investigate the function of Arf6 in mediating cellular morphogenesis during early sea urchin development.
- To dissect Arf6's role in the migration and differentiation of primary mesenchyme cells (PMCs) and endodermal cells.
Main Methods:
- Utilized loss-of-function morpholino injections to inhibit Arf6 activity.
- Employed a constitutively active Arf6-Q67L construct to study its gain-of-function effects.
- Focused on sea urchin embryos, specifically examining PMCs and endodermal cells.
Main Results:
- Arf6 is essential for skeleton formation and primary mesenchyme cell migration, attributed to its actin remodeling capabilities.
- Arf6 loss-of-function leads to gastrulation defects.
- Constitutively active Arf6 causes endodermal cell detachment and reduced cadherin staining, suggesting a role in cadherin recycling.
Conclusions:
- Arf6 plays a significant role in embryonic morphogenesis by regulating actin dynamics and cell-cell adhesion.
- Arf6 impacts coordinated cell movements critical for the formation of embryonic structures.
- Arf6's involvement in cadherin recycling is crucial for maintaining epithelial integrity during development.
Related Concept Videos
Mechanism of Lamellipodia Formation
3.9K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.9K
Small GTPases - Ras and Rho
5.6K
Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Three regulatory proteins control their activity:
5.6K
Generation of Straight or Branched Actin Filaments
3.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.9K
GTPases and their Regulation
10.2K
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
Large G-proteins,...
10.2K
GTPases and their Regulation
3.1K
3.1K
Coat Assembly and GTPases
4.6K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.6K


