2014
DOI: 10.1002/cbic.201300715
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The Surprising Features of the TEAD4‐Vgll1 Protein–Protein Interaction

Abstract: The Hippo signaling pathway, which controls organ size in animals, is altered in various human cancers. The TEAD transcription factors, the most downstream elements in this pathway, are regulated by different cofactors, such as the Vgll (vestigial-like) proteins. Having studied the interaction between Vgll1-derived peptides and human TEAD4, we show that, although it lacks a key secondary structure element required for tight binding by two other TEAD cofactors (YAP and TAZ), Vgll1-derived peptides bind to TEAD … Show more

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Cited by 30 publications
(62 citation statements)
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“…This conserved residue, which does not belong to the α‐helix but to the preceding loop, was included to enhance the solubility of the peptides. In agreement with published results, 1 has a low micromolar potency while 2 does not show any activity in the assay (Table ). This could be linked to a different level of pre‐organization of these peptides in their unbound state.…”
Section: Resultssupporting
confidence: 92%
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“…This conserved residue, which does not belong to the α‐helix but to the preceding loop, was included to enhance the solubility of the peptides. In agreement with published results, 1 has a low micromolar potency while 2 does not show any activity in the assay (Table ). This could be linked to a different level of pre‐organization of these peptides in their unbound state.…”
Section: Resultssupporting
confidence: 92%
“…Since the lateral chains of the residues from the β‐strand and loop regions of hYAP and mVGLL1/4 have a limited role in the interaction with TEAD, differences in affinity for TEAD between their β‐strand:loop:α‐helix motif should come essentially from their α‐helix region. This is indeed the case for the α‐helices of hYAP and mVGLL1 which show a potency lower than 150 µM and around 4 µM, respectively . The large difference in affinity between the isolated α‐helices of mVGLL1 and hYAP is intriguing since both of them bind in a very similar fashion to the same region on the TEAD surface .…”
Section: Introductionmentioning
confidence: 69%
“…The peptides are N‐acetylated and C‐amidated and to minimize oxidation, their methionine residues were replaced with norleucine (noted x). A peptide derived from murine VGLL 1 was used because it has a higher solubility than its human counterpart under our experimental conditions .…”
Section: Resultsmentioning
confidence: 99%
“…B). Peptides mimicking only the β‐strand:α‐helix region from YAP have a low affinity (>150 μ m ) for TEAD, while equivalent VGLL1 peptides bind with good affinity (100–150 n m ) to this transcription factor . The presence of the Ω‐loop is thus a prerequisite for tight binding of YAP (and TAZ) and for competing effectively with VGLL.…”
Section: Discussionmentioning
confidence: 99%
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