Conformational changes in the Arp2/3 complex leading to actin nucleation

Rodal, Avital A.; Sokolova, Olga; Robins, Deborah B; Daugherty, Karen M; Hippenmeyer, Simon; Riezman, Howard; Grigorieff, Nikolaus; Goode, Bruce L.

doi:10.1038/nsmb870

Cited by 164 publications

(231 citation statements)

References 26 publications

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“…The mechanism of activation of Las17 is unclear. However, once activated it is thought that Las17 binds to and activates Arp2/3 that in turn initiates actin polymerization at the site (Winter et al, 1999;Rodal et al, 2005). The formation of branched and bundled actin structures at the patch have been shown to be critical for the invagination process (Galletta et al, 2008;Gheorghe et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

The WASP Homologue Las17 Activates the Novel Actin-regulatory Activity of Ysc84 to Promote Endocytosis in Yeast

Robertson¹,

Allwood²,

Smith³

et al. 2009

MBoC

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Actin plays an essential role in many eukaryotic cellular processes, including motility, generation of polarity, and membrane trafficking. Actin function in these roles is regulated by association with proteins that affect its polymerization state, dynamics, and organization. Numerous proteins have been shown to localize with cortical patches of yeast actin during endocytosis, but the role of many of these proteins remains poorly understood. Here, we reveal that the yeast protein Ysc84 represents a new class of actin-binding proteins, conserved from yeast to humans. It contains a novel N-terminal actin-binding domain termed Ysc84 actin binding (YAB), which can bind and bundle actin filaments. Intriguingly, full-length Ysc84 alone does not bind to actin, but binding can be activated by a specific motif within the polyproline region of the yeast WASP homologue Las17. We also identify a new monomeric actin-binding site on Las17. Together, the polyproline region of Las17 and Ysc84 can promote actin polymerization. Using live cell imaging, kinetics of assembly and disassembly of proteins at the endocytic site were analyzed and reveal that loss of Ysc84 and its homologue Lsb3 decrease inward movement of vesicles consistent with a role in actin polymerization during endocytosis.

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Section: Introductionmentioning

confidence: 99%

The WASP Homologue Las17 Activates the Novel Actin-regulatory Activity of Ysc84 to Promote Endocytosis in Yeast

Robertson¹,

Allwood²,

Smith³

et al. 2009

MBoC

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show abstract

“…In chemotaxing ctxA/B null cells, coronin localized at the leading edge as in wild-type cells. These results indicate that the localization of coronin, which binds to the Arp2/3 complex and inhibits nucleation activity of the complex (Rodal et al, 2005), is not affected by the absence of cortexillins.…”

Section: Localization Of Gfp-coronin In Ctxa/b Null Cellsmentioning

confidence: 76%

“…2A). To determine whether cortexillins are localized at the F-actin assembly sites, the localization of GFP-cortexillin I was compared with that of a newly formed F-actin marker protein GFP-coronin (Gerisch et al, 1995), which associates with the Arp2/3 complex on F-actin filaments and inhibits actin nucleation (Rodal et al, 2005). The majority of GFP-coronin was found at protruding regions as clearly accumulated forms (Fig.…”

Section: Subcellular Localization Of Cortexillin Imentioning

confidence: 99%

“…To understand temporal translocation kinetics of cortexillin I in more detail, the cell cortex translocation kinetics of cortexillin I were compared with those of other F-actin binding proteins such as ArpD, a subunit of Arp2/3 complex (Rodal et al, 2005), and coronin and PhdA-GFP (Funamoto et al, 2002), a pleckstrin homology domain containing PIP3 reporter (Fig. 3C).…”

Section: Subcellular Localization Of Cortexillin Imentioning

confidence: 99%

“…The Arp2/3 complex directly nucleates actin assembly and forms new branch points. Efficient actin nucleation requires its interactions with WASP family members, which are Cdc42 and Rac effectors (Raftopoulou and Hall, 2004), and/or a pre-existing actin filament (Firat-Karalar and Welch, 2011;Raftopoulou et al, 2004;Rodal et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Dynamic Localization of the Actin-Bundling Protein Cortexillin I during Cell Migration

Cha

Jeon

2011

Molecules and Cells

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Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization in Dictyostelium. Here, we investigated dynamic subcellular localization of cortexillin I in chemotaxing Dictyostelium cells. Most of the cortexillin I was enriched on the lateral sides of moving cells. Upon chemoattractant stimulation, cortexillin I was rapidly released from the cortex followed by a transient translocation to the cell cortex with a peak at ~5 s and a subsequent decrease to basal levels, indicating that localization of cor-texillin I at the cortex in chemotaxing cells is controlled by two more signaling components, one for the initial delocalization from the cortex and another for the translocation to the cortex ~5 s after chemoattractant stimulation. Loss of cortexillins leads to reduced cell polarity and an in-creased number of lateral pseudopodia during chemotaxis, suggesting that cortexillins play an inhibitory role in producing pseudopodia along the lateral sides of the cell. Cells lacking cortexillins displayed extended chemoattrac-tantmediated Arp2/3 complex translocation kinetics to the cortex. Our present study provides a new insight into the function of cortexillins during reorganization of the actin cytoskeleton and cell migration.

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Deletion of gmfA induces keratocyte‐like migration inDictyostelium

et al. 2021

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Glia maturation factor (GMF) has been established as an inactivating factor of the actin‐related protein 2/3 (Arp2/3) complex, which regulates actin assembly. Regulation of actin assembly and reorganization is crucial for various cellular events, such as cell migration, cell division, and development. Here, to examine the roles of ADF‐H domain‐containing protein (also known as glia maturation factor; GmfA), the product of a single GMF homologous gene in Dictyostelium , gmfA‐null cells were generated. They had moderate defects in cell growth and cytokinesis. Interestingly, they showed a keratocyte‐like fan shape with a broader pseudopod, where Arp3 accumulated at higher levels than in wild‐type cells. They migrated with higher persistence, but their velocities were comparable to those of wild‐type cells. The polar pseudopods during cell division were also broader than those in wild‐type cells. However, GmfA did not localize at the pseudopods in migrating cells or the polar pseudopods in dividing cells. Adhesions of mutant cells to the substratum were much stronger than that of wild‐type cells. Although the mutant cells showed chemotaxis comparable to that of wild‐type cells, they formed disconnected streams during the aggregation stage; however, they finally formed normal fruiting bodies. These results suggest that GmfA plays a crucial role in cell migration.

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Conformational changes in the Arp2/3 complex leading to actin nucleation

Cited by 164 publications

References 26 publications

The WASP Homologue Las17 Activates the Novel Actin-regulatory Activity of Ysc84 to Promote Endocytosis in Yeast

The WASP Homologue Las17 Activates the Novel Actin-regulatory Activity of Ysc84 to Promote Endocytosis in Yeast

Dynamic Localization of the Actin-Bundling Protein Cortexillin I during Cell Migration

Deletion of gmfA induces keratocyte‐like migration inDictyostelium

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