ArticleJournal of molecular biology2011
High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activation.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- De novo-designed transmembrane proteins bind and regulate a cytokine receptor.Nature chemical biology · 2024Article
- Cytosolic Delivery of Bioactive Cyclic Peptide Cargo by Spontaneous Membrane Translocating Peptides.ACS omega · 2024Article
- Synthetic Molecular Evolution of Cell Penetrating Peptides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Applications and evolution of melittin, the quintessential membrane active peptide.Biochemical pharmacology · 2021Review
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Application of Synthetic Molecular Evolution to the Discovery of Antimicrobial Peptides.Advances in experimental medicine and biology · 2019Review
- Synthetic molecular evolution of hybrid cell penetrating peptides.Nature communications · 2018Article
- Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes.Biochimica et biophysica acta · 2014Article
- Tie2 and Eph receptor tyrosine kinase activation and signaling.Cold Spring Harbor perspectives in biology · 2014Review
- The pathogenic A391E mutation in FGFR3 induces a structural change in the transmembrane domain dimer.The Journal of membrane biology · 2013Article
- Synthetic molecular evolution of pore-forming peptides by iterative combinatorial library screening.ACS chemical biology · 2013Article
- Article
- Extracellular assembly and activation principles of oncogenic class III receptor tyrosine kinases.Nature reviews. Cancer · 2012Review
- Gain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Journal of the American Chemical Society · 2012Article
- Transmembrane helix dimerization: beyond the search for sequence motifs.Biochimica et biophysica acta · 2012Review
- Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence.Scientific reports · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Dimerization is a critical requirement for the activation of the intracellular kinase domains of receptor tyrosine kinases (RTKs). The single transmembrane (TM) helices of RTKs contribute to dimerization, but the details are not well understood. Work with TM helices in various model systems has revealed a small number of specific dimerization sequence motifs, and it has been suggested that RTK dimerization is modulated by such motifs. Yet questions remain about the universality of these sequence motifs for RTK dimerization and about how TM domain dimerization in model systems relates to RTK activation in mammalian membranes. To investigate these questions, we designed a 3888-member combinatorial peptide library based on the TM domain of Neu (ErbB2) as a model RTK. The library contains many closely related, Neu-like sequences, including thousands of sequences with known dimerization motifs. We used an SDS-PAGE-based screen to select peptides that dimerize better than the native Neu sequence, and we assayed the activation of chimeric Neu receptors in mammalian cells with TM sequences selected in the screen. Despite the very high abundance of known dimerization motifs in the library, only a very few dimerizing sequences were identified by SDS-PAGE. About half of those sequences activated the Neu kinase significantly more than did the wild-type TM sequence. This work furthers our knowledge about the requirements for membrane protein interactions and the requirements for RTK activation in cells.
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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.