Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?

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Architecture and Membrane Interactions of the EGF Receptor

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A liquid phase of synapsin and lipid vesicles

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Regulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3ɛ Cytoplasmic Tyrosine-Based Motif

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Mechanism of Activation of Protein Kinase JAK2 by the Growth Hormone Receptor

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RALA and RALBP1 regulate mitochondrial fission at mitosis

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The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins

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Intrinsic disorder in scaffold proteins: Getting more from less

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The Lateral Organization and Mobility of Plasma Membrane Components

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Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy

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Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif

Pérez-Jover, I., Rochon, K., Hu, D., Mahajan, M. K., Mohan, P. M., Santos-Pérez, I., Gisasola, J. O., Galvez, J. M. M., Agirre, J., Qi, X., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44413-6 · Cited by 15 · see citing works

The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection

Vieira, M. F. M., Hernandez, G., Zhong, Q., Arbesú, M., Veloso, T., Gomes, T., Martins, M. L., Monteiro, H., Frazão, C., Frankel, G., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05856-9 · Cited by 14 · see citing works

Quartz crystal microbalance and atomic force microscopy to characterize mimetic systems based on supported lipids bilayer

Fructuoso-Bonet, N., Cava, D. G., & Vélez, M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.935376 · Cited by 14 · see citing works

CoMemMoRFPred: Sequence-based Prediction of MemMoRFs by Combining Predictors of Intrinsic Disorder, MoRFs and Disordered Lipid-binding Regions

Basu, S., Hegedűs, T., & Kurgan, L. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168272 · Cited by 14 · see citing works

Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci

(2025) · doi:10.1038/s41467-025-58692-8 · Cited by 14 · see citing works

Remodeling of the Plasma Membrane by Surface-Bound Protein Monomers and Oligomers: The Critical Role of Intrinsically Disordered Regions

Araya, M. K., Zhou, Y., & Gorfe, A. A. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00256-8 · Cited by 14 · see citing works

Membrane Association of Intrinsically Disordered Proteins

MacAinsh, M., Muhammedkutty, F. N. K., Prasad, R., & Zhou, H. (2025) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070124-092816 · Cited by 13 · see citing works

Synthesis and Preliminary Characterization of Putative Anle138b-Centered PROTACs against α-Synuclein Aggregation

Pedrini, M., Iannielli, A., Meneghelli, L., Passarella, D., Broccoli, V., & Seneci, P. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15051467 · Cited by 13 · see citing works

The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation

Has, C., & Das, S. L. (2023) · The Journal of Membrane Biology · doi:10.1007/s00232-023-00289-7 · Cited by 13 · see citing works

Folding of N-terminally acetylated α-synuclein upon interaction with lipid membranes

Tang, Z., Fang, Z., Wu, X., Liu, J., Tian, L., Li, X., Diao, J., Ji, B., & Li, D. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.09.019 · Cited by 13 · see citing works

Phosphatidylserine and Phosphatidylethanolamine Asymmetry Have a Negligible Effect on the Global Structure, Dynamics, and Interactions of the KRAS Lipid Anchor

Araya, M. K., & Gorfe, A. A. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c01253 · Cited by 10 · see citing works

Conformational ensemble-dependent lipid recognition and segregation by prenylated intrinsically disordered regions in small GTPases

Araya, M. K., & Gorfe, A. A. (2023) · Communications Biology · doi:10.1038/s42003-023-05487-6 · Cited by 9 · see citing works

Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach

Singh, A. J., Padariya, M., Faktor, J., Kote, S., Mikac, S., Dziadosz, A., Lam, T. W., Brydon, J., Wear, M. A., Ball, K. L., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-21393-z · Cited by 8 · see citing works

An inducible amphipathic α-helix mediates subcellular targeting and membrane binding of RPE65

Uppal, S., Liu, T., Galvan, E., Gomez, F., Tittley, T., Poliakov, E., Gentleman, S., & Redmond, T. M. (2022) · Life Science Alliance · doi:10.26508/lsa.202201546 · Cited by 8 · see citing works

RLIP76: A Structural and Functional Triumvirate

Cornish, J., Owen, D., & Mott, H. R. (2021) · Cancers · doi:10.3390/cancers13092206 · Cited by 8 · see citing works

Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs

Chamberlain, S. G., Gohlke, A., Shafiq, A., Squires, I. J., Owen, D., & Mott, H. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2104219118 · Cited by 7 · see citing works

Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential

Novikova, O. D., Uversky, V. N., & Zelepuga, E. (2021) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2021.06.012 · Cited by 7 · see citing works

Simulations reveal a balance between protein–protein and protein–lipid interactions during condensation on membrane surfaces

Zinga, K., Lee, Y., Pathak, S., Patel, N., Stachowiak, J. C., & Ren, P. Y. (2025) · Chemical Science · doi:10.1039/d5sc04862a · Cited by 6 · see citing works

Heterodimerization domains in MAP4 KINASEs determine subcellular localization and activity in Arabidopsis

Pan, L., de Lima, C. F. F., Vu, L. D., van de Cotte, B., Winne, N. D., Gevaert, K., Jaeger, G. D., & Smet, I. D. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae176 · Cited by 5 · see citing works

Structural molecular details of the endocytic adaptor protein CALM upon binding with phosphatidylinositol 4,5-bisphosphate-containing model membranes

Santamaría, A., Pereira, D., Pawar, N., Kelly, B. T., Carrascosa-Tejedor, J., Sardo, M., Mafra, L., Fragneto, G., Owen, D. J., Marín-Montesinos, I., et al. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01590-3 · Cited by 5 · see citing works

From disorder comes function: Regulation of small GTPase function by intrinsically disordered lipidated membrane anchor

Hutchins, C. M., & Gorfe, A. A. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102869 · Cited by 5 · see citing works

Exploring the Role of Anionic Lipid Nanodomains in the Membrane Disruption and Protein Folding of Human Islet Amyloid Polypeptide Oligomers on Lipid Membrane Surfaces Using Multiscale Molecular Dynamics Simulations

Nguyen, N., Lewis, A., Pham, T. L. H., Sikazwe, D., & Cheng, K. H. (2023) · Molecules · doi:10.3390/molecules28104191 · Cited by 5 · see citing works

Basic Residue Clusters in Intrinsically Disordered Regions of Peripheral Membrane Proteins: Modulating 2D Diffusion on Cell Membranes

Pons, M. (2021) · Physchem · doi:10.3390/physchem1020010 · Cited by 5 · see citing works

Host-encoded ETP2 is involved in recruiting the dynamin-like protein ETP9 to the endosymbiont division site in trypanosomatid Angomonas deanei

Maurya, A. K., Cadena, L. R., Ehret, G., & Nowack, E. C. M. (2025) · mBio · doi:10.1128/mbio.02247-25 · Cited by 4 · see citing works

Mycobacterium tuberculosis uses intrinsically disordered, fast evolving proteins to interact with conserved host factors

Pozzoli, U., Forni, D., Arrigoni, F., Cagliani, R., GIOIA, L. D., & Sironi, M. (2025) · Genome biology · doi:10.1186/s13059-025-03854-6 · Cited by 4 · see citing works

Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers

Byrd, E. J., Norgate, E. L., Crossley, J. A., Chau, C. C. C., Schiffrin, B., Kulak, A. N., Radford, S. E., Actis, P., Calabrese, A. N., & Sobott, F. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c00544 · Cited by 4 · see citing works

Vibration influence on the O2-dependent processes activity in human erythrocytes

Доценко, О. И., Mischenko, А. М., & Taradina, G. V. (2021) · Regulatory Mechanisms in Biosystems · doi:10.15421/022162 · Cited by 3 · see citing works

Biochemical and NMR studies reveal specific interaction between STIMATE C-tail and PI(4,5)P2 or PI(3,4,5)P3-containing membrane

Liu, C., Zhang, Y., Ge, L., Li, L., Wu, B., & Wang, J. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.01.100 · Cited by 2 · see citing works

Intrinsically disordered proteins in viral pathogenesis and infections

Selvaraj, C., Pravin, M. A., Alhoqail, W. A., Nayarisseri, A., & Singh, S. K. (2022) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2022.06.002 · Cited by 2 · see citing works

Enhanced sampling for lipid-protein interactions during membrane dynamics

Masone, D. (2022) · Biocell · doi:10.32604/biocell.2023.024146 · Cited by 2 · see citing works

Buffer-dependent conformational dynamics of α-synuclein revealed by nanopipette electrospray ionisation ion mobility mass spectrometryPreprint

Byrd, E. J., Norgate, E. L., Crossley, J. A., Chau, C. C. C., Schiffrin, B., Kulak, A. N., Radford, S. E., Actis, P., Calabrese, A. N., & Sobott, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.19.671163 · Cited by 2 · see citing works

The penta-EF-hand protein Pef1 of Candida albicans functions at sites of membrane perturbation to support polarized growth and membrane integrity

Weichert, M., Schumann, M. R., Brandt, U., Bedford, C., Brand, A., & Fleißner, A. (2026) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkag075 · Cited by 1 · see citing works

Membrane extraction by calmodulin underpins the disparate signalling of RalA and RalB

Chamberlain, S. G., Owen, D., & Mott, H. R. (2022) · BioEssays · doi:10.1002/bies.202200011 · Cited by 1 · see citing works

Unravelling the role of the A domain and N-terminal alpha-helices of FtsY in archaeal signal recognition particle

Gupta, S., Sinha, S., Bhakta, K., Bhowmick, A., & Ghosh, A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141645 · Cited by 1 · see citing works

The pathogen-encoded signaling receptor Tir exploits host-like intrinsic disorder to assist infectionPreprint

Vieira, M. F. M., Hernández, G., Veloso, T., Monteiro, H., Arbesú, M., Zanzoni, A., & Cordeiro, T. N. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.22.440577 · Cited by 1 · see citing works

Interaction Between Proteins and Biological Membranes

Janosi, L., & Gorfe, A. A. (2022) · doi:10.1002/9783527830503.ch13 · Cited by 1 · see citing works

Heterogeneity of Signaling Complex Nanostructure in T Cells Activated Via the T Cell Antigen Receptor

Barr, V. A., Piao, J., Balagopalan, L., McIntire, K. M., Schoenberg, F. P., & Samelson, L. E. (2023) · Microscopy and Microanalysis · doi:10.1093/micmic/ozad072

Allosteric control of dynamin-related protein 1-catalyzed mitochondrial fission through a conserved disordered C-terminal Short Linear MotifPreprint

Pérez-Jover, I., Rochon, K., Hu, D., Mohan, P. M., Santos-Pérez, I., Gisasola, J. O., Galvez, J. M. M., Agirre, J., Qi, X., Mears, J. A., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-3161608/v1

Structural analysis and functional evaluation of the disordered ß–hexosyltransferase region from Hamamotoa (Sporobolomyces) singularis

Dagher, S. F., Vaishnav, A., Stanley, C. B., Meilleur, F., Edwards, B. F. P., & Bruno-Bárcena, J. M. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1291245

Formation of Amyloid-Like Conformational States of β-Structured Membrane Proteins on the Example of OMPF Porin from the Yersinia pseudotuberculosis Outer Membrane

Novikova, O. D., Rybinskaya, T. V., Zelepuga, E., Uversky, V. N., Kim, N. Y., Chingizova, E. A., Menchinskaya, E. S., Хоменко, В. А., Chistyulin, D. K., & Portnyagina, O. Y. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924060087

The penta-EF-hand protein Pef1 of Candida albicans functions at sites of membrane perturbation to support polarized growth and membrane integrityPreprint

Weichert, M., Schumann, M. R., Brandt, U., Brand, A., & Fleißner, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.06.611525

Interplay of proteins and lipids during endoplasmic reticulum-associated protein degradation

Vrentzou, A. (2024) · doi:10.53846/goediss-10873

Formation of Amyloid-Like Conformational States of β-Structured Membrane Proteins on the Example of the OmpF Porin from the Yersinia pseudotuberculosis Outer Membrane

Novikova, O. D., Rybinskaya, T. V., Zelepuga, E., Uversky, V. N., Kim, N. Y., Chingizova, E. A., Menchinskaya, E. S., Хоменко, В. А., Chistyulin, D. K., & Portnyagina, O. Y. (2024) · Biochemistry (Moscow) · doi:10.31857/s0320972524060081

A novel host-encoded protein, ETP2, plays an important role in endosymbiont division in the trypanosomatid Angomonas deaneiPreprint

Maurya, A. K., Cadena, L. R., Ehret, G., & Nowack, E. C. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.22.649992

Membrane-associated intrinsically disordered regions: dual roles in binding and membrane protein function

Poskin, L., Bâlon, H., Leyder, T., Michaux, C., & Mignon, J. (2026) · Critical Insights in Biophysics · doi:10.1080/29932203.2026.2638665

Structural characterisation of the interaction between the nsP3 protein of CHIKV and FHL1

Ferrino-Iriarte, A. (2022) · theses.fr (ABES) · doi:10.70675/75c91464z8478z4f4dz8161z101645cc36fd

Lipoengineering of Biomolecular Condensates Controls Material Properties and Multiphase Hierarchy to Guide Organoid MorphogenesisPreprint

Huang, Z., Alam, M. M., Shokri, M., Savitrinarayana, H. C., Sisila, V., Agarwal, T., Scrutton, R. M., Maryam, L., Gulzar, A., Wang, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.08.717265

Cell Membrane Targeting via Spacer Length-Engineered Amphiphilic DNA Frameworks

Zhou, Z., Qian, J., Liang, C. F., Yang, J., Zhou, Y., Duan, M., Li, Z., Shen, J., & Luo, S. (2026) · ACS Applied Bio Materials · doi:10.1021/acsabm.6c00321

Metal-induced energy transfer uncovers activation-induced axial reorganization of signaling complexes inside cellsPreprint

Wienbeuker, E., Felker, A., Nevskyi, O., Harms, S. T., Marx, D., Tanzusch, K., Chizhik, A. M., Kurre, R., You, C., Enderlein, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.23.719849

Energetic landscapes and fuzzy complexes: Computational targeting of viral intrinsically disordered proteins

Viknesh, K., Vijayalakshmi, P., Alex, A. M., Muthumani, L. N., Muthupandian, S., Desai, D., Ramanathan, S., Likson, A., & Selvaraj, C. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.04.009

amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome

Lobo, S., Griem, L., Shell, M. S., & Shea, J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2531932123

Loss of ZmDMP increases phosphatidic acid production and disrupts lipid homeostasis in maize sperm cells

Yao, S., Zhang, Z., Tang, S., Liu, H., Yang, B., & Wang, X. (2026) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiag427

N-Terminal Amine Chemistry Influences α-Synuclein Interactions with Lipid Bilayers

Brackhahn, E. A. E., Li, M.-H., Miranda-Castrodad, P., Lee, H., Musila, J., Eliezer, D., & Rhoades, E. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00382

Patchy Membrane-Directed Multiphase Complex Coacervation

Sun, S., Erkamp, N. A., Huisman, S. G. A. M., Cook, A. B., Nikroo, A. H., Yin, Z., Wang, J., Verwiel, M. A. M., & van Hest, J. C. M. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c11826

Intrinsically disordered regions in the NLRP family of receptors act as regulatory hubs for inflammasome condensation and activation

Nava-Ramírez, T., Cuevas‐Velazquez, C. L., Covarrubias, A. A., Rudiño-Piñera, E., Pérez‐Martínez, L., & Pedraza‐Alva, G. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1793320

OPC3/LEW: A New Flexible Three-Site Water Model to Simulate Low-Electrostatic Environments

Romero-Figueroa, J. R., Aguilar-Pineda, J. A., & González-Melchor, M. (2026) · ACS Omega · doi:10.1021/acsomega.6c08432

Intrinsically disordered proteins play diverse roles in cell signaling

Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222 · see citing works

Functions of intrinsic disorder in transmembrane proteins

Kjærgaard, M., & Kragelund, B. B. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2562-5 · Cited by 90 · see citing works

On the roles of intrinsically disordered proteins and regions in cell communication and signaling

Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00774-3 · Cited by 109 · see citing works

Intrinsically disordered proteins in cellular signalling and regulation

Wright, P. E., & Dyson, H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3920 · Cited by 2,371 · see citing works

Choreography by Structural Disorder in Membrane Proteins

Kragelund, B. B. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2016.11.095