ArticlePloS one2012
Protein disorder and short conserved motifs in disordered regions are enriched near the cytoplasmic side of single-pass transmembrane proteins.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Discovery and design of potent cell surface display elements.Nature biotechnology · 2026Article
- Electromagnetic Field Stimulation Effects on Intrinsically Disordered Proteins and Their Role in Aging and Neurodegeneration.Journal of biomedical science and engineering · 2025Article
- The relative binding position of Nck and Grb2 adaptors impacts actin-based motility of Vaccinia virus.eLife · 2022Article
- Production of an Active, Human Membrane Protein inInternational journal of molecular sciences · 2022Article
- Integrative structural dynamics probing of the conformational heterogeneity in synaptosomal-associated protein 25.Cell reports. Physical science · 2021Article
- Short Disordered Epitope of CRTAM Ig-Like V Domain as a Potential Target for Blocking Antibodies.International journal of molecular sciences · 2020Article
- The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.The Journal of membrane biology · 2019Review
- HH-MOTiF: de novo detection of short linear motifs in proteins by Hidden Markov Model comparisons.Nucleic acids research · 2017Article
- Article
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Cadherin juxtamembrane region derived peptides inhibit TGFβ1 induced gene expression.Bioarchitecture · 2014Article
- The eukaryotic linear motif resource ELM: 10 years and counting.Nucleic acids research · 2014Article
- Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins.Biochimica et biophysica acta · 2013Review
- Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.PloS one · 2013Article
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Authors and funding
6 authors.
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Abstract
Intracellular juxtamembrane regions of transmembrane proteins play pivotal roles in cell signalling, mediated by protein-protein interactions. Disordered protein regions, and short conserved motifs within them, are emerging as key determinants of many such interactions. Here, we investigated whether disorder and conserved motifs are enriched in the juxtamembrane area of human single-pass transmembrane proteins. Conserved motifs were defined as short disordered regions that were much more conserved than the adjacent disordered residues. Human single-pass proteins had higher mean disorder in their cytoplasmic segments than their extracellular parts. Some, but not all, of this effect reflected the shorter length of the cytoplasmic tail. A peak of cytoplasmic disorder was seen at around 30 residues from the membrane. We noted a significant increase in the incidence of conserved motifs within the disordered regions at the same location, even after correcting for the extent of disorder. We conclude that elevated disorder within the cytoplasmic tail of many transmembrane proteins is likely to be associated with enrichment for signalling interactions mediated by conserved short motifs.
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