Abl tyrosine kinases regulate cell–cell adhesion through Rho GTPases

Zandy, Nicole Lynn; Playford, Martin P.; Pendergast, Ann Marie

doi:10.1073/pnas.0703077104

Cited by 121 publications

(148 citation statements)

References 44 publications

Supporting

Mentioning

138

Contrasting

Order By: Relevance

“…And finally, maintenance and stabilization of adherence junctions is achieved by downregulation of actin turnover at the contact points (Pilot et al, 2006;Zandy et al, 2007). A B…”

Section: Cell-cell Interactions In Establishment Of Pcpmentioning

confidence: 99%

Controlled levels of canonical Wnt signaling are required for neural crest migration

Maj

Künneke

Loresch

et al. 2016

Developmental Biology

View full text Add to dashboard Cite

“…And finally, maintenance and stabilization of adherence junctions is achieved by downregulation of actin turnover at the contact points (Pilot et al, 2006;Zandy et al, 2007). A B…”

Section: Cell-cell Interactions In Establishment Of Pcpmentioning

confidence: 99%

Controlled levels of canonical Wnt signaling are required for neural crest migration

Maj

Künneke

Loresch

et al. 2016

Developmental Biology

View full text Add to dashboard Cite

“…2 show that Sos1 silencing results in alteration of macrophage cytoskeleton dynamics similar to those reported in cells where Abl, or Src-family kinases, were deficient or inhibited (14,15,18). The established relation among Abl, Src, and Rac in different cell context (17,28,36,(40)(41)(42)(43) prompted experiments to address whether Sos1 silencing affects Rac activation.…”

Section: Sos1 Regulates Cytoskeleton Dynamics In Macrophagesmentioning

confidence: 99%

Sos1 Regulates Macrophage Podosome Assembly and Macrophage Invasive Capacity

Baruzzi

Remelli

Lorenzetto

et al. 2015

The Journal of Immunology

View full text Add to dashboard Cite

Podosomes are protrusive structures implicated in macrophage extracellular matrix degradation and three-dimensional migration through cell barriers and the interstitium. Podosome formation and assembly are regulated by cytoskeleton remodeling requiring cytoplasmic tyrosine kinases of the Src and the Abl families. Considering that Abl has been reported to phosphorylate the guanine nucleotide exchange factor Sos1, eliciting its Rac-guanine nucleotide exchange factor activity, and Rac regulates podosome formation in myeloid cells and invadopodia formation in cancer cells, we addressed whether Sos1 is implicated in podosome formation and function in macrophages. We found that ectopically expressed Abl or the Src kinase Fgr phosphorylate Sos1, and the Src kinases Hck and Fgr are required for Abl and Sos1 phosphorylation and Abl/Sos1 interaction in macrophages. Sos1 localizes to podosomes in both murine and human macrophages, and its silencing by small interfering RNA results in disassembly of murine macrophage podosomes and a marked reduction of GTP loading on Rac. Matrix degradative capacity, three-dimensional migration through Matrigel, and transmigration through an endothelial cell monolayer of Sos1-silenced macrophages were inhibited. In addition, Sos1- or Abl-silenced macrophages, or macrophages treated with the selective Abl inhibitor imatinib mesylate had a reduced capability to migrate into breast tumor spheroids, the majority of cells remaining at the margin and the outer layers of the spheroid itself. Because of the established role of Src and Abl kinases to regulate also invadopodia formation in cancer cells, our findings suggest that targeting the Src/Abl/Sos1/Rac pathway may represent a double-edged sword to control both cancer-invasive capacities and cancer-related inflammation.

show abstract

“…Abl-family kinases are stimulated by a variety of upstream stimuli, including growth factors (Furstoss et al, 2002;Plattner et al, 2003;Plattner et al, 1999;Plattner et al, 2004), cellmatrix and cell-cell adhesion (Hernandez et al, 2004;Huang et al, 2008;Lewis et al, 1996;Renshaw et al, 2000;Zandy et al, 2007), DNA damage (Kharbanda et al, 1995), oxidative stress (Cao et al, 2001;Sun et al, 2000), and bacterial invasion (Backert et al, 2008;Burton et al, 2005;Newsome et al, 2006;Poppe et al, 2007;Tammer et al, 2007). Exciting recent work has identified several mechanisms that involve both receptors and soluble proteins that enhance Abl and Arg kinase activity, and these are discussed below.…”

Section: Pathways That Activate Abl-family Kinasesmentioning

confidence: 99%

Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts

Bradley

Koleske

2009

Journal of Cell Science

159

206

View full text Add to dashboard Cite

The Abl-family non-receptor tyrosine kinases are essential regulators of the cytoskeleton. They transduce diverse extracellular cues into cytoskeletal rearrangements that have dramatic effects on cell motility and morphogenesis. Recent biochemical and genetic studies have revealed several mechanisms that Abl-family kinases use to mediate these effects. Abl-family kinases stimulate actin polymerization through the activation of cortactin, hematopoietic lineage cell-specific protein (HS1), WASp-and WAVE-family proteins, and Rac1. They also attenuate cell contractility by inhibiting RhoA and altering adhesion dynamics. These pathways impinge on several physiological processes, including development and maintenance of the nervous and immune systems, and epithelial morphogenesis. Elucidating how Abl-family kinases are regulated, and where and when they coordinate cytoskeletal changes, is essential for garnering a better understanding of these complex processes.

show abstract

Abl tyrosine kinases regulate cell–cell adhesion through Rho GTPases

Cited by 121 publications

References 44 publications

Controlled levels of canonical Wnt signaling are required for neural crest migration

Controlled levels of canonical Wnt signaling are required for neural crest migration

Sos1 Regulates Macrophage Podosome Assembly and Macrophage Invasive Capacity

Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts

Contact Info

Product

Resources

About