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NHERF1 is a PDZ-domain adapter protein that stabilizes its binding partners at the plasma membrane.
First, it is important to consider that zebrafish and human Dystrophin differ at amino acid level and hence the affinity of the human protein might be lower to its binding partners at the zebrafish sarcolemma.
The identification of new binding partners – at the cell membrane, in the cytoplasm and in the nucleus – as well as the characterization of the post-translational modification patterns will bring new insights into this aspect of the Notch network.
However, this conclusion was supported by work largely performed in heterologous cell over-expression systems and was arrived at before the identification of CFTR binding partners at the N- and C-termini [ 27- 34].
Based on the in vitro binding of vezatin to the FERM domains of radixin (this study) and myosin VIIa (Küssel-Andermann et al, 2000), vezatin binding partners at the junctions between HCs and their SCs may include not only radixin and myosin VIIa, but also other unconventional myosins with FERM tail domains (myosins VIIb, X, XVa) (Oliver et al, 1999) that could be present at these junctions.
The observation that mutation or deletion of genes encoding membrane and membrane-associated components of the SPB can be suppressed by elimination of Ndc1 binding partners at the NPC such as Pom152 or Pom34 has led to the idea that the SPB and NPC may compete for Ndc1 or other NE insertion factors (Chial et al. 1998; Sezen et al. 2009; Witkin et al. 2010; Casey et al. 2012).
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We identify Nup153 as an important impβ binding partner at the nuclear face of the pore.
This may explain why even proteins such as PfHRPII that have no clear binding partner at the host skeleton nonetheless seem to be restricted to the periphery of the infected erythrocyte.
This is used here, for example, to achieve straight actin filament segments by placing an free actin binding to a barbed end of a filamentous actin directly opposite (i.e., at a relative angle of 180°) the latter's already present binding partner at the pointed end.
Thus, the functional assay shown in Figure 6D provides evidence that 7xAla/L107C NEMO retains the ability to productively interact with key binding partners at sites up and down its length.
The active recruitment and de-recruitment of HAT and HDAC enzymes and their binding partners at sites of DNA damage produces localized sites of open chromatin, increasing the genotoxic effectiveness of agents such as UV, IR, and chemotherapeutic agents.
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