ArticleBiochemistry2016
Topologically Diverse Human Membrane Proteins Partition to Liquid-Disordered Domains in Phase-Separated Lipid Vesicles.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes.Nature communications · 2024Article
- Strength in numbers: effect of protein crowding on the shape of cell membranes.Biochemical Society transactions · 2022Review
- Malaria parasites release vesicle subpopulations with signatures of different destinations.EMBO reports · 2022Article
- The Two Faces of the Liquid Ordered Phase.The journal of physical chemistry letters · 2022Article
- Ion mobility-mass spectrometry reveals the role of peripheral myelin protein dimers in peripheral neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Peripheral myelin protein 22 preferentially partitions into ordered phase membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Temperature Dependence of the Structure and Dynamics of a Dye-Labeled Lipid in a Planar Phospholipid Bilayer: A Computational Study.The Journal of membrane biology · 2019Article
- Reduced level of docosahexaenoic acid shifts GPCR neuroreceptors to less ordered membrane regions.PLoS computational biology · 2019Article
- Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018Review
- Phase Composition Control in Microsphere-Supported Biomembrane Systems.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- The C99 domain of the amyloid precursor protein resides in the disordered membrane phase.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The integration of membrane proteins into "lipid raft" membrane domains influences many biochemical processes. The intrinsic structural properties of membrane proteins are thought to mediate their partitioning between membrane domains. However, whether membrane topology influences the targeting of proteins to rafts remains unclear. To address this question, we examined the domain preference of three putative raft-associated membrane proteins with widely different topologies: human caveolin-3, C99 (the 99 residue C-terminal domain of the amyloid precursor protein), and peripheral myelin protein 22. We find that each of these proteins are excluded from the ordered domains of giant unilamellar vesicles containing coexisting liquid-ordered and liquid-disordered phases. Thus, the intrinsic structural properties of these three topologically distinct disease-linked proteins are insufficient to confer affinity for synthetic raft-like domains.
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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.