Interaction of Cortactin and N-WASp with Arp2/3 Complex

Weaver, Alissa M.; Heuser, John E.; Karginov, Andrei V.; Lee, Wei lih; Parsons, J. Thomas; Cooper, John A.

doi:10.1016/s0960-9822(02)01035-7

Cited by 243 publications

(310 citation statements)

References 38 publications

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“…6A), suggesting that Arp2 does not contribute significantly to the binding affinity of Arp2/3 complex with VCA. Previous cross-linking results also implicated Arp3 in Arp2/3 interaction with VCA (7,8); however, the GST-VCA beads exhibited the same level of interaction with the Arp2/3 complex in ⌬arp3 extracts as that in wild-type extracts (Fig. 6C).…”

Section: Arpc1/arc40 Functions In Budding Yeastmentioning

confidence: 60%

“…For the following analysis, we used the GST-VCA and GST-VCA W503A peptides from N-WASP because the mutant and wild-type N-WASP-VCA peptides were characterized previously for binding to the Arp2/3 complex (26). Mutations affecting the conserved tryptophan in the A region were previously shown to disrupt the interaction of VCA with the Arp2/3 complex (8,26). As shown in Fig.…”

Section: Arpc1/arc40 Functions In Budding Yeastmentioning

confidence: 91%

“…A potential involvement of ARPC1 in activator interaction has been suggested by previous chemical cross-linking experiments, which showed that VCA can be cross-linked to ARPC1, Arp2, and Arp3 (7,8). Interestingly one study concluded that the COOH-terminal conserved tryptophan of VCA is involved in binding to Arp3 because truncating the DDW motif from the VCA COOH terminus reduced cross-linking to Arp3 by 81% and to ARPC1 by 37% (8).…”

Section: Arpc1/arc40 Functions In Budding Yeastmentioning

confidence: 94%

“…Despite this wealth of data, we currently still lack direct insights into the nature of the conformation change induced by contacts with VCA and F-actin and how various subunits contribute to this change. Chemical cross-linking experiments showed that three subunits, Arp2, Arp3, and ARPC1, are in close contact with VCA (7,8). However, these results do not necessarily imply that all three subunits contain binding sites for VCA or indicate the extent to which each subunit contributes to the interaction between the complex and VCA.…”

mentioning

confidence: 88%

“…For binding His 6 -HA-Arc40, ϳ40 l of GST-N-WASP-VCA-, GST-N-WASP-VCA W503A -, and GST protein-bound beads (1.75 M) and 1.5, 3, and 4.5 M purified Arc40 were mixed in a total volume of 200 l; or 40 l of yeast Myo5-CA-or GST-Bee1-VCA-bound beads (1.75 M) and 1.5 M purified Arc40 were mixed in a total volume of 200 l. For binding Arp2/3 complex from yeast extract, 5 l of GST-VCA beads were mixed with variable amounts of high speed extracts or purified Arp2/3 complex in a total volume of 200 l. K d was determined as described previously (8). Briefly GST-VCA-coated Affi-Gel beads (0 -8 M) were incubated with 250 nM purified His 6 -HA-Arc40 or 200 nM Arp2/3 complex in 1ϫ UBA buffer ϩ 2 mg/ml bovine serum albumin.…”

Section: Recombinant Protein Expression and Purification-gst-taggedmentioning

confidence: 99%

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ARPC1/Arc40 Mediates the Interaction of the Actin-related Protein 2 and 3 Complex with Wiskott-Aldrich Syndrome Protein Family Activators

Pan

Égile

Lipkin

et al. 2004

Journal of Biological Chemistry

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The actin-related protein 2 and 3 (Arp2/3) complex is a seven-subunit protein complex that nucleates actin filaments at the cell cortex. Despite extensive cross-linking, crystallography, genetic and biochemical studies, the contribution of each subunit to the activity of the complex remains largely unclear. In this study we characterized the function of the 40-kDa subunit, ARPC1/ Arc40, of the yeast Arp2/3 complex. We showed that this subunit is indeed a stable component of the Arp2/3 complex, but its highly unusual electrophoretic mobility eluded detection in previous studies. Recombinant Arc40 bound the VCA domain of Wiskott-Aldrich syndrome protein family activators at a K d of 0.45 M, close to that of the full complex with VCA (0.30 M), and this interaction was dependent on the conserved tryptophan at the COOH terminus of VCA. Using a newly constructed ⌬arc40 yeast strain, we showed that loss of Arc40 severely reduced the binding affinity of the Arp2/3 complex with VCA as well as the nucleation activity of the complex, suggesting that Arc40 contains an important contact site of the Arp2/3 complex with VCA. The ⌬arc40 cells exhibited reduced growth rate, loss of actin patches, and accumulation of cables like actin aggregates, phenotypes typical of other subunit nulls, suggesting that Arc40 functions exclusively within the Arp2/3 complex.

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Section: Arpc1/arc40 Functions In Budding Yeastmentioning

confidence: 60%

Section: Arpc1/arc40 Functions In Budding Yeastmentioning

confidence: 91%

Section: Arpc1/arc40 Functions In Budding Yeastmentioning

confidence: 94%

mentioning

confidence: 88%

Section: Recombinant Protein Expression and Purification-gst-taggedmentioning

confidence: 99%

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ARPC1/Arc40 Mediates the Interaction of the Actin-related Protein 2 and 3 Complex with Wiskott-Aldrich Syndrome Protein Family Activators

Pan

Égile

Lipkin

et al. 2004

Journal of Biological Chemistry

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Cortactin branches out: Roles in regulating protrusive actin dynamics

Ammer

Weed

2008

Cell Motil. Cytoskeleton

240

262

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Since its discovery in the early 1990's, cortactin has emerged as a key signaling protein in many cellular processes, including cell adhesion, migration, endocytosis, and tumor invasion. While the list of cellular functions influenced by cortactin grows, the ability of cortactin to interact with and alter the cortical actin network is central to its role in regulating these processes. Recently, several advances have been made in our understanding of the interaction between actin and cortactin, providing insight into how these two proteins work together to provide a framework for normal and altered cellular function. This review examines how regulation of cortactin through post-translational modifications and interactions with multiple binding partners elicits changes in cortical actin cytoskeletal organization, impacting the regulation and formation of actin-rich motility structures. Cell Motil. Cytoskeleton 65: 687-707, 2008. '

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Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions

Ren

Crampton

Yap

2009

Cell Motil. Cytoskeleton

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It has long been recognized that adhesion receptors cooperate with the cytoskeleton during morphogenesis, tissue remodeling and homeostasis. But how this occurs is less well-understood. A host of cytoskeletal regulators have been reported to have functional and biochemical linkage with adhesion receptors. The challenge remains to find functionally-coherent patterns within this increasingly large corpus of molecular information. In this review we discuss one approach, to identify distinctive functional modules that contribute to different adhesive processes. We illustrate this by considering Arp2/3-driven surface protrusion, which is utilized at both integrin-based cell-matrix adhesions and cadherin-based cell-cell adhesions. We further argue that regulatory proteins, such as cortactin, serve to coordinate the molecular components of this protrusive apparatus into a cohesive module. Cell Motil. Cytoskeleton 66: 865-873, 2009. '

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Interaction of Cortactin and N-WASp with Arp2/3 Complex

Cited by 243 publications

References 38 publications

ARPC1/Arc40 Mediates the Interaction of the Actin-related Protein 2 and 3 Complex with Wiskott-Aldrich Syndrome Protein Family Activators

ARPC1/Arc40 Mediates the Interaction of the Actin-related Protein 2 and 3 Complex with Wiskott-Aldrich Syndrome Protein Family Activators

Cortactin branches out: Roles in regulating protrusive actin dynamics

Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions

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