ArticlePloS one2016
Intrinsic Disorder in Transmembrane Proteins: Roles in Signaling and Topology Prediction.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 81 citations in OpenAlex.
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- Structural and functional implications of phase separation of membrane protein LacY in Escherichia coli.Nature communications · 2026Article
- APOL1 plasma membrane pools resist rapid protein degradation.Scientific reports · 2026Article
- Comparative assessment of binding residue predictions in intrinsically disordered regions.Protein science : a publication of the Protein Society · 2025Article
- The effects of retinal disease on intrinsic protein disorder and liquid-liquid‑phase separation.Journal of proteins and proteomics · 2025Article
- Investigations on genomic, topological and structural properties of diguanylate cyclases involved inCurrent research in structural biology · 2025Article
- Beyond Static Tethering at Membrane Contact Sites: Structural Dynamics and Functional Implications of VAP Proteins.Molecules (Basel, Switzerland) · 2025Review
- Prediction of Intrinsically Disordered Lipid Binding Residues with DisoLipPred.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering.The EMBO journal · 2024Article
- ER Stress Decreases Gene Expression Of Transmembrane Protein 117 Via Activation of PKR-like ER Kinase.Cell biochemistry and biophysics · 2023Article
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- Homotypic SCOTIN assemblies form ER-endosome membrane contacts and regulate endosome dynamics.EMBO reports · 2023Article
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- Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro.Plant direct · 2023Article
- Effects of the anti-inflammatory drug celecoxib on cell death signaling in human colon cancer.Naunyn-Schmiedeberg's archives of pharmacology · 2023Article
- Initial Investigations of Intrinsically Disordered Regions in Inherited Retinal Diseases.International journal of molecular sciences · 2023Article
- Structural analysis and functional evaluation of the disordered ß-hexosyltransferase region fromFrontiers in bioengineering and biotechnology · 2023Article
- Disease association and comparative genomics of compositional bias in human proteins.F1000Research · 2023Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered regions (IDRs) are peculiar stretches of amino acids that lack stable conformations in solution. Intrinsic Disorder containing Proteins (IDP) are defined by the presence of at least one large IDR and have been linked to multiple cellular processes including cell signaling, DNA binding and cancer. Here we used computational analyses and publicly available databases to deepen insight into the prevalence and function of IDRs specifically in transmembrane proteins, which are somewhat neglected in most studies. We found that 50% of transmembrane proteins have at least one IDR of 30 amino acids or more. Interestingly, these domains preferentially localize to the cytoplasmic side especially of multi-pass transmembrane proteins, suggesting that disorder prediction could increase the confidence of topology prediction algorithms. This was supported by the successful prediction of the topology of the uncharacterized multi-pass transmembrane protein TMEM117, as confirmed experimentally. Pathway analysis indicated that IDPs are enriched in cell projection and axons and appear to play an important role in cell adhesion, signaling and ion binding. In addition, we found that IDP are enriched in phosphorylation sites, a crucial post translational modification in signal transduction, when compared to fully ordered proteins and to be implicated in more protein-protein interaction events. Accordingly, IDPs were highly enriched in short protein binding regions called Molecular Recognition Features (MoRFs). Altogether our analyses strongly support the notion that the transmembrane IDPs act as hubs in cellular signal events.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.