Detection of protein-protein interactions in plants using the transrepressive activity of the EAR motif repression domain [PDF]
The Plant Journal, 2010 The activities of many regulatory factors involve interactions with other proteins. We demonstrate here that the ERF-associated amphiphilic repression (EAR) motif repression domain (SRDX) can convert a transcriptional complex into a repressor via transrepression that is mediated by protein-protein interactions and show that transrepressive activity of ...
Kyoko, Matsui, Masaru, Ohme-Takagi
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p160/SRC/NCoA coactivators form complexes via specific interaction of their PAS-B domain with the CID/AD1 domain [PDF]
, 2008 Transcriptional activation involves the ordered recruitment of coactivators via direct interactions between distinct binding domains and recognition motifs.
Coudevylle, N. +12 more
core +1 more source
PDZ domains and their binding partners: structure, specificity, and modification
Cell Communication and Signaling, 2010 PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins. They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction ...
Zheng Jie J, Lee Ho-Jin
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The LSD1-type zinc finger motifs of Pisum sativa LSD1 are a novel nuclear localization signal and interact with importin alpha. [PDF]
PLoS ONE, 2011 BACKGROUND: Genetic studies of the Arabidopsis mutant lsd1 highlight the important role of LSD1 in the negative regulation of plant programmed cell death (PCD).
Shanping He +5 more
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Mapping of domain-mediated protein-protein interaction by SPOT peptide assay
STAR Protocols, 2021 Summary: Identification of peptides mediating protein-protein interaction (PPI) is crucial for understanding the function of interlinked proteins in cellular processes and amino acid-associated diseases.
Xiaoyi Mao +4 more
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Novel modular domain PB1 recognizes PC motif to mediate functional protein–protein interactions [PDF]
The EMBO Journal, 2001 Modular domains mediating specific protein-protein interactions play central roles in the formation of complex regulatory networks to execute various cellular activities. Here we identify a novel domain PB1 in the budding yeast protein Bem1p, which functions in polarity establishment, and mammalian p67(phox), which activates the microbicidal phagocyte ...
T, Ito +4 more
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Versatile Site-Selective Protein Reaction Guided by WW Domain–Peptide Motif Interaction [PDF]
Bioconjugate Chemistry, 2017 A short, flexible, and unstructured peptide tag that has versatile and facile use in protein labeling applications is highly desirable. Here, we report an 11-residue peptide tag with an internal cysteine (a W-tag, derived from a Comm PY peptide motif that is known to bind with Nedd4 WW3* domain) that can be installed at different regions of the target ...
Miao Liu +3 more
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Rewiring MAP kinases in Saccharomyces cerevisiae to regulate novel targets through ubiquitination
eLife, 2016 Evolution has often copied and repurposed the mitogen-activated protein kinase (MAPK) signaling module. Understanding how connections form during evolution, in disease and across individuals requires knowledge of the basic tenets that govern kinase ...
Benjamin Groves +4 more
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Peptide array X-linking (PAX): a new peptide-protein identification approach. [PDF]
PLoS ONE, 2012 Many protein interaction domains bind short peptides based on canonical sequence consensus motifs. Here we report the development of a peptide array-based proteomics tool to identify proteins directly interacting with ligand peptides from cell lysates ...
Hirokazu Okada +5 more
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Cells, 2021 SH3 domains constitute an important class of protein modules involved in a variety of cellular functions. They participate in protein-protein interactions via their canonical ligand binding interfaces composed of several evolutionarily conserved aromatic
Orsolya Tőke +6 more
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