The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration

Suraneni, Praveen; Rubinstein, Boris; Unruh, Jay R.; Durnin, Michael; Hanein, Dorit; Li, Rong

doi:10.1083/jcb.201112113

Cited by 307 publications

(342 citation statements)

References 73 publications

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“…This result is consistent with data from other cells where ARP2 is required for normal directional movement. 55 In agreement with the microarray data, WASp showed significantly altered expression in the peritoneum compared to the blood (Figure 3). Apoptosis plays an important role in the neutrophil cycle with involvement in continuation or resolution of the inflammatory response.…”

Section: Discussionsupporting

confidence: 76%

Neutrophil transcriptional profile changes during transit from bone marrow to sites of inflammation

et al. 2014

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Section: Discussionsupporting

confidence: 76%

Neutrophil transcriptional profile changes during transit from bone marrow to sites of inflammation

et al. 2014

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“…2). Cells expressing protrusive structures, such as lamellipodia and filopodia, are generally more adhesive to a solid substratum and have a larger cell surface under microscopic observation than those without them (25). We therefore carried out morphometric analysis of cell surface area to measure cell spreading (Fig.…”

Section: Biologicalmentioning

confidence: 99%

A Putative Polypeptide N-Acetylgalactosaminyltransferase/Williams-Beuren Syndrome Chromosome Region 17 (WBSCR17) Regulates Lamellipodium Formation and Macropinocytosis

Nakayama

Nakamura

Oki

et al. 2012

Journal of Biological Chemistry

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Background: WBSCR17 is a potential polypeptide N-acetylgalactosaminyltransferase with unknown function. Results: WBSCR17, induced with N-acetylglucosamine, regulated O-glycosylation, lamellipodium formation, and macropinocytosis. Conclusion: Mucin-type O-glycosylation may be involved in lamellipodium formation and membrane trafficking through macropinocytosis. Significance: The data suggest that mucin-type O-glycosylation modulates the dynamic membrane transport of the cell and may be involved in the control of nutrient uptake.

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“…Roles for Membrane Binding and Lamellipodia in Cell Migration-Lamellipodia are not important for cell migration in wound healing and several other settings (43)(44)(45)(46). Examples include CP-binding mutants of CARMIL1 or CARMIL2, which show little or no defect in collective cell migration despite the loss of lamellipodia (22,43).…”

Section: Discussionmentioning

confidence: 99%

Cell Migration and Invadopodia Formation Require a Membrane-binding Domain of CARMIL2

Lanier¹,

McConnell

Cooper

2016

Journal of Biological Chemistry

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CARMILs regulate capping protein (CP), a critical determinant of actin assembly and actin-based cell motility. Vertebrates have three conserved CARMIL genes with distinct functions. In migrating cells, CARMIL2 is important for cell polarity, lamellipodial assembly, ruffling, and macropinocytosis. In cells, CARMIL2 localizes with a distinctive dual pattern to vimentin intermediate filaments and to membranes at leading edges and macropinosomes. The mechanism by which CARMIL2 localizes to membranes has not been defined. Here, we report that CARMIL2 has a conserved membrane-binding domain composed of basic and hydrophobic residues, which is necessary and sufficient for membrane localization, based on expression studies in cells and on direct binding of purified protein to lipids. Most important, we find that the membrane-binding domain is necessary for CARMIL2 to function in cells, based on rescue expression with a set of biochemically defined mutants. CARMIL1 and CARMIL3 contain similar membrane-binding domains, based on sequence analysis and on experiments, but other CPI motif proteins, such as CD2AP, do not. Based on these results, we propose a model in which the membrane-binding domain of CARMIL2 tethers this multidomain protein to the membrane, where it links dynamic vimentin filaments with regulation of actin assembly via CP.

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The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration

Abstract: Embryonic stem cell–derived fibroblasts with genetic disruption of the Arp2/3 complex are unable to form lamellipodia or undergo sustained directional migration.

Cited by 307 publications

References 73 publications

Neutrophil transcriptional profile changes during transit from bone marrow to sites of inflammation

Neutrophil transcriptional profile changes during transit from bone marrow to sites of inflammation

A Putative Polypeptide N-Acetylgalactosaminyltransferase/Williams-Beuren Syndrome Chromosome Region 17 (WBSCR17) Regulates Lamellipodium Formation and Macropinocytosis

Cell Migration and Invadopodia Formation Require a Membrane-binding Domain of CARMIL2

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