The conserved C-terminal I/LWEQ module targets Talin1 to focal adhesions.

@article{Franco2006TheCC,
  title={The conserved C-terminal I/LWEQ module targets Talin1 to focal adhesions.},
  author={Santos J. Franco and Melissa A Senetar and William T. N. Simonson and Anna Huttenlocher and Richard O. McCann},
  journal={Cell motility and the cytoskeleton},
  year={2006},
  volume={63 9},
  pages={
          563-81
        }
}
The cytoskeletal protein Talin1 is a critical link between integrins and the actin cytoskeleton, where it is required for the structural and signaling functions of integrin-containing adhesion complexes. However, the elements in Talin1 that are responsible for localizing it to adhesion complexes are not known. In this report we have used a series of constructs based on the modular structure of Talin1 to determine the structural elements that specify the subcellular localization of Talin1. We… 
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Evidence that talin alternative splice variants from Ciona intestinalis have different roles in cell adhesion
TLDR
Vertebrates and D. discoideum contain two talin genes that encode proteins with different functions, which suggests that multicellular organisms require multiple talins as components of adhesion complexes.
Control of High Affinity Interactions in the Talin C Terminus
TLDR
It is concluded that several bundles of the C terminus cooperate to regulate targeting and concomitantly tailor high affinity interactions of the talin rod in cell adhesions.
Distinct developmental roles for direct and indirect talin-mediated linkage to actin.
The Integrin Binding Site 2 (IBS2) in the Talin Rod Domain Is Essential for Linking Integrin β Subunits to the Cytoskeleton*
TLDR
The minimal structure of IBS2 is determined and it is shown that this integrin binding site corresponds to 23 residues located in α helix 50 of the talin rod domain (residues 2077-2099), providing the first direct evidence that IBS1 in the talIn rod is essential to link integrins to the cytoskeleton.
Structural model and functional significance of pH-dependent talin–actin binding for focal adhesion remodeling
TLDR
A molecular mechanism for pH-sensitive actin binding by talin is identified and FA turnover is suggested to be pH-dependent and in part mediated by pH- dependent affinity of talin for binding actin.
Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin
TLDR
It is found that neither talin nor vinculin alone recruit actin filaments to the membrane, which indicates that the local membrane composition plays a key role in controlling the stepwise recruitment, activation, and engagement of proteins within FAs.
Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle.
TLDR
The results suggest thatTalin1 is the primary link between integrins and actin in dynamic focal adhesions in undifferentiated, motile cells, but that Talin2 may serve as the link between integrates and the sarcomeric cytoskeletonin stable adhesion complexes in mature striated muscle.
Mutations in the Drosophila alphaPS2 integrin subunit uncover new features of adhesion site assembly.
Mutations in the Drosophila α PS 2 integrin subunit uncover new features of adhesion site assembly
TLDR
Although talin recruitment requires αPS2βPS, talin levels are not simply specified by the amount of integrin at the adhesive junction, suggesting that the integrin–talin link is weaker than the ECM-integrin link.
Talin1 Regulates TCR-Mediated LFA-1 Function1
TLDR
It is indicated that TCR-induced up-regulation of LFA-1-dependent adhesiveness and resulting T cell-APC conjugation require talin1.
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References

SHOWING 1-10 OF 97 REFERENCES
Characterization of an actin-binding site within the talin FERM domain.
Conformation, Localization, and Integrin Binding of Talin Depend on Its Interaction with Phosphoinositides*
TLDR
The results demonstrate that activation of the integrin-binding activity of talin requires not only integrin engagement to the extracellular matrix but also the binding of PI4,5P2 to talin, suggesting a possible role of lipid metabolism in organizing the sequential assembly of focal adhesion components.
Layilin, A Novel Talin-binding Transmembrane Protein Homologous with C-type Lectins, is Localized in Membrane Ruffles
TLDR
A new binding partner for talin is reported, which contains homology with C-type lectins, is present in numerous cell lines and tissue extracts, and is expressed on the cell surface, and a short region within talin's amino-terminal 435 amino acids capable of binding to layilin in vitro is identified.
The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals.
  • R. O. McCann, S. Craig
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
TLDR
The results establish the location of an F-actin binding domain in native talin, demonstrate that direct interaction of Sla2 with actin is a possible basis for its effect on the actin cytoskeleton in vivo, and define the I/LWEQ consensus as a new actin-binding motif.
Sequence and domain structure of talin
TLDR
A model for the structure of talin is described based on this sequence and other data, which define a novel family of submembranous cytoskeleton-associated proteins all apparently involved in connections to the plasma membrane.
Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin.
TLDR
The affinity of the I/LWEQ module proteins Talin1, Talin2, huntingtin interacting protein-1 (Hip1), and the Hip1-related protein (H hip1R/Hip12) for F-actin is determined and a conserved structural element is identified that interferes with the actin binding capacity of these proteins.
Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals.
TLDR
It is established by immunolocalization that Sla2p is a component of the yeast cortical actin cytoskeleton, and two intramolecular interactions mediated by coiled-coil domains appear to contribute to the regulation of Sla1p distribution between the cytoplasm and plasma membrane.
Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site.
TLDR
The results suggest that, although both the N- and C-terminal regions of talin bind actin, the properties of these two regions of the protein are distinct.
Localization of an Integrin Binding Site to the C Terminus of Talin*
TLDR
Results indicate that an integrin binding site is located within residues 1984–2541 of the talin rod domain, one in the homologous FERM (band four-point-one, ezrin,radixin, moesin) domain and another near its C terminus.
Mapping and Consensus Sequence Identification for Multiple Vinculin Binding Sites within the Talin Rod*
TLDR
The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration and the specificity of this interaction is defined by spot-synthesizing a series of 25-mer talin VBS1 peptides containing substitutions with all the commonly occurring amino acids.
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5
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