Integrin cytoplasmic domains as connectors to the cell's signal transduction apparatus

LaFlamme, Susan E.; Homan, Suzanne M.; Bodeau, Amy L.; Mastrangelo, Anthony

doi:10.1016/s0945-053x(97)90003-2

Cited by 53 publications

(30 citation statements)

References 57 publications

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“…It therefore remains to be determined whether it is the common region or the unique 12 amino acids of ␤ 1B that mediates the observed signal response that results in recruitment of talin, VASP, and the p130Cas-Crk-Dock180 scaffold and activation of Rac1. Neither can it be excluded that the ␣-chain of the integrin receptor contributes to the observed effects, since ␣-chains also mediate certain signaling (1,3,76). It is also possible that the state of integrin activation and/or the clustering capacity influences the outcome of receptor ligation.…”

Section: Discussionmentioning

confidence: 99%

Temporal Dissection of β1-Integrin Signaling Indicates a Role for p130Cas-Crk in Filopodia Formation

Gustavsson¹,

Yuan

Fällman

2004

Journal of Biological Chemistry

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Invasin-promoted spreading of ␤ 1 -integrin-deficient cells, transfected with the ␤ 1A -or ␤ 1B -integrin splice variants, were used to dissect early ␤ 1 -integrin signaling events. The ␤ 1B isoform, which has a different membrane-distal part of the cytoplasmic tail from ␤ 1A , is defective in signaling and function. When plated on surfaces coated with the high affinity ligand invasin, ␤ 1B -integrin-expressing cells spread by forming filopodia with distinct adhesive phosphotyrosine complexes at the tips, without signs of lamellipodia. This suggested that the ␤ 1B -integrin mediated a partial signaling sufficient for formation of filopodia but insufficient for lamellipodia formation. When screening for proteins present in the distal filopodial phosphotyrosine complexes of ␤ 1B cells, p130Cas and the filopodia proteins vasodilator-stimulated phosphoprotein and talin were found, whereas the typical focal complex proteins focal adhesion kinase, paxillin, and vinculin were not. Invasinpromoted adhesion induced complex formation of p130Cas and the adapter Crk. Moreover, Crk together with Dock180 were present at the filopodial tips of ␤ 1B -integrin-expressing cells, and there was a prominent Rac1 activation. Expression of dominant negative variants of p130Cas or CrkII blocked ␤ 1B -integrin-mediated filopodia formation, indicating that this signaling scaffold is central in this process.

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Section: Discussionmentioning

confidence: 99%

Temporal Dissection of β1-Integrin Signaling Indicates a Role for p130Cas-Crk in Filopodia Formation

Gustavsson¹,

Yuan

Fällman

2004

Journal of Biological Chemistry

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“…Integrins provide physical linkage between the cytoskeleton and ECM and they transduce signals initiated by extracellular interactions [33]. The a-integrin subunits have diverse amino acid sequences and distinct functions [33].…”

Section: Discussionmentioning

confidence: 99%

Epidermal Growth Factor Enhances Invasive Activity of BeWo Choriocarcinoma Cells by Inducing .ALPHA.2 Integrin Expression

et al. 2003

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Abstract. The trophoblast, an important component of the mammalian placenta, has several essential biological roles in the maintenance of pregnancy. First, trophoblast cells must attach to the uterine endometrium, and then they must invade to a depth at which the vascular network exists. Here, we investigated the effects of epidermal growth factor (EGF) on a2 integrin expression, adhesiveness to collagen, and invasive activity using human BeWo choriocarcinoma cells. EGF induced the expression of a2 integrin mRNA and protein, as shown by Northern blotting, Western blotting, and flow cytometry. Human chorionic gonadotropin (hCG) secretion was enhanced by the addition of EGF, which suggests that the BeWo cells functionally differentiated similarly to normal trophoblasts. EGF also dose-dependently stimulated the invasiveness of BeWo cells. Antibody against a2 integrin inhibited this effect, suggesting that it may be mediated by an increase of cell surface integrin. EGF had no effect on the adhesiveness of BeWo cells to collagen, whereas it stimulated the chemokinetic activity in a dose-dependent manner. The increase of chemokinetic activity was suppressed by antibody against a2 integrin. These results suggest that EGF may induce a2 integrin expression in trophoblast cells, thereby enhancing their invasiveness into the endometrium via an increase of their chemokinetic activity.

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“…Deletions or mutations of these two domains, in particular of the tyrosine residues at position 747 and 759, cause loss of cell adhesion, migration, and integrin localization to focal adhesions, as well as decreased recruitment and activation of FAK. [38][39][40] Likewise, a point mutation of serine 752 inhibits 'inside-out' and 'outside-in' signaling. 41 Intracellular delivery of a peptide containing the NITY sequence was shown to inhibit ␣V␤3-but not ␤1-dependent cell adhesion.…”

Section: U/ml Of Adcmvch2 (A-e) or Adcmvch1 (F-k) After 7 H Cells Wmentioning

confidence: 99%

Disruption of integrin-dependent adhesion and survival of endothelial cells by recombinant adenovirus expressing isolated β integrin cytoplasmic domains

Oguey

Rüegg

2000

Gene Ther

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We explored the possibility of using a genetic approach to inhibit integrin-mediated endothelial cell adhesion and survival. We constructed recombinant adenoviruses (Ads) expressing chimeric proteins consisting of the cytoplasmic and transmembrane domains of integrin ␤1 (CH1), ␤3 (CH3) or the ␤1 transmembrane domain alone (CH2) connected to the extracellular domain of L3T4 placed under the control of the CMV promoter (AdCMV) or the endothelial cell specific Tie-1 promoter (AdTie). All constructs were expressed in a dose-and time-dependent manner with over 90% of cells expressing the constructs within 24 h (AdCMVs) or 72 h (AdTies) after infection. Confluent monolayers of HUVEC infected with AdCMVCH1 or AdCMVCH3 detached from the substrate in a time-and dose-dependent manner with over

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Integrin cytoplasmic domains as connectors to the cell's signal transduction apparatus

Cited by 53 publications

References 57 publications

Temporal Dissection of β1-Integrin Signaling Indicates a Role for p130Cas-Crk in Filopodia Formation

Temporal Dissection of β1-Integrin Signaling Indicates a Role for p130Cas-Crk in Filopodia Formation

Epidermal Growth Factor Enhances Invasive Activity of BeWo Choriocarcinoma Cells by Inducing .ALPHA.2 Integrin Expression

Disruption of integrin-dependent adhesion and survival of endothelial cells by recombinant adenovirus expressing isolated β integrin cytoplasmic domains

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