Background: The Scar/WAVE family of proteins mediates signals to actin assembly by direct activation of the Arp2/3 complex. These proteins have been characterised as major regulators of lamellipodia formation downstream of Rac activation and as members of large protein complexes.
Results: We have investigated the interactions of the three human Scar/WAVE isoforms with several previously described binding partners for Scar/WAVE 1 or 2. We find that all three Scar/WAVE isoforms behave similarly and are likely to participate in the same kinds of protein complexes that regulate actin assembly.
Conclusion: Differences between Scar/WAVE proteins are therefore likely to be at the level of tissue distribution or subtle differences in the affinity for specific binding partners.
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| http://dx.doi.org/10.1186/1471-2121-6-11 | DOI Listing |
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WAVE1 and WAVE2 have distinct and overlapping roles in controlling actin assembly at the leading edge.
Mol Biol Cell
September 2020
Department of Biology, Brandeis University, Waltham, MA 02454.
Article Synopsis
- SCAR/WAVE proteins, specifically WAVE1 and WAVE2, work together at the cell's leading edge to form branched actin networks essential for cell movement.
- Research shows that while both isoforms are necessary for creating lamellipodia, WAVE1 uniquely regulates the rate of actin extension, with WAVE2 compensating for its absence.
- The study highlights that WAVE1 plays a crucial role in linking actin networks to the cell membrane, influencing how cells extend their protrusions despite being redundant in some functions with WAVE2.
Scar/WAVE3 contributes to motility and plasticity of lamellipodial dynamics but not invasion in three dimensions.
Biochem J
November 2012
The Beatson Institute for Cancer Research, Garscube Estate, Switchback Rd., Bearsden, Glasgow G61 1BD, UK.
Article Synopsis
- The Scar/WAVE complex helps cells move around by activating something called the Arp2/3 complex, which makes cell parts called actin branch out and form extensions.
- In a study, when a part called Scar/WAVE3 was removed from breast cancer cells, the cells moved slower and had bigger but less active edges called lamellipodia.
- However, Scar/WAVE3 didn't seem to affect the cells' ability to invade through thicker materials, showing that how they move in flat spaces isn't as important in 3D environments.
Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties.
J Cell Sci
May 2007
School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
Article Synopsis
- - IRSp53 is a scaffold protein involved in actin filament bundling and interacts with small GTPases Rac and Cdc42, as well as Scar/WAVE and Mena/VASP proteins to regulate the actin cytoskeleton.
- - Researchers identified a similar protein, IRTKS, which is widely distributed, acts as a substrate for the insulin receptor, and interacts with Rac, but does not bind to Cdc42.
- - IRTKS leads to the formation of short actin bundles instead of filopodia-like protrusions, possibly due to a unique short carboxyl-terminal (Ct) extension that alters actin organization, though it doesn’t seem to sequester actin monomers like
Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2.
BMC Cell Biol
March 2005
School of Biosciences, The University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Background: The Scar/WAVE family of proteins mediates signals to actin assembly by direct activation of the Arp2/3 complex. These proteins have been characterised as major regulators of lamellipodia formation downstream of Rac activation and as members of large protein complexes.
Results: We have investigated the interactions of the three human Scar/WAVE isoforms with several previously described binding partners for Scar/WAVE 1 or 2.
Loss of WAVE-1 causes sensorimotor retardation and reduced learning and memory in mice.
Proc Natl Acad Sci U S A
February 2003
Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
The Scar/WAVE family of scaffolding proteins organize molecular networks that relay signals from the GTPase Rac to the actin cytoskeleton. The WAVE-1 isoform is a brain-specific protein expressed in variety of areas including the regions of the hippocampus and the Purkinje cells of the cerebellum. Targeted disruption of the WAVE-1 gene generated mice with reduced anxiety, sensorimotor retardation, and deficits in hippocampal-dependent learning and memory.
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