2012
DOI: 10.1083/jcb.201202041
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Tiam1 interaction with the PAR complex promotes talin-mediated Rac1 activation during polarized cell migration

Abstract: The PAR complex targets Tiam1 to adhesions, where it interacts with talin to promote adhesion-induced Rac1 activation, cell spreading, and migration.

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Cited by 67 publications
(84 citation statements)
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References 53 publications
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“…Inhibiting ROCK leads to the loss of mature focal adhesions; however, these cells can still consistently undergo haptotaxis. Rac1, Tiam1, SFKs and FAK all localize to focal complexes (Mitra and Schlaepfer, 2006;Rottner et al, 1999;Wang et al, 2012), and are all required for haptotaxis, further implicating focal complexes as the main adhesion complex required for fibronectin haptotaxis. Because many other cell types that lack mature focal adhesions exhibit integrin-containing structures similar to focal complexes, haptotactic responses might be a characteristic of many cell types (Weber et al, 2013).…”
Section: Discussion a Working Model For Haptotaxismentioning
confidence: 99%
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“…Inhibiting ROCK leads to the loss of mature focal adhesions; however, these cells can still consistently undergo haptotaxis. Rac1, Tiam1, SFKs and FAK all localize to focal complexes (Mitra and Schlaepfer, 2006;Rottner et al, 1999;Wang et al, 2012), and are all required for haptotaxis, further implicating focal complexes as the main adhesion complex required for fibronectin haptotaxis. Because many other cell types that lack mature focal adhesions exhibit integrin-containing structures similar to focal complexes, haptotactic responses might be a characteristic of many cell types (Weber et al, 2013).…”
Section: Discussion a Working Model For Haptotaxismentioning
confidence: 99%
“…These structures also contain both Tiam1 and Rac1 (Boissier and Huynh-Do, 2014;Wang et al, 2012), along with clustered integrins, and are strong candidates for the adhesion structures required for haptotaxis in the place of mature focal adhesions. SFK and FAK signaling originates at focal complexes (Mitra and Schlaepfer, 2006) and, consistent with this, we observed active FAK and Src ( phosphorylated FAK and Src) at focal complexes, as well as at lower levels at focal adhesions ( decreased the activating phosphorylation of FAK and Src (without altering the total levels), respectively, and also altered the localization of the adhesions (Fig.…”
Section: Differential Lamellipodial Protrusion Dynamics Regulate Haptmentioning
confidence: 99%
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“…Beyond this, the F3 subdomain has emerged as showing remarkable ligand‐binding plasticity and has been linked to binding FAK 31, TIAM1 (T‐cell lymphoma invasion and metastasis 1) 65, layilin 66, Gα13 (G‐protein subunit Galpha13 ) and RIAM 67 all via the same site. The hierarchy of these interactions, that are presumably mutually exclusive with integrin binding and each other, is not yet fully understood.…”
Section: Structure Of Talin 1 Andmentioning
confidence: 99%
“…3 H and I); therefore PLEKHG3 is not the only RhoGEF that is activated by PI3K to induce cell polarity. In addition to PLEKHG3, PI3K might regulate other GEFs that can also activate Rac1, such as guanine nucleotide exchange factor VAV2 (32) or T-lymphoma invasion and metastasis 1 (TIAM1) (3,33,34), to induce cell polarity and migration. Based on the findings described above, we propose a tentative model for how PLEKHG3 pathways enhance cell polarity and cell migration.…”
Section: Plekhg3 Enhances Polarized Cell Migration Via a Positive Feementioning
confidence: 99%