A dynamic partitioning mechanism polarizes membrane protein distribution
Tatsat Banerjee (),
Satomi Matsuoka,
Debojyoti Biswas,
Yuchuan Miao,
Dhiman Sankar Pal,
Yoichiro Kamimura,
Masahiro Ueda,
Peter N. Devreotes () and
Pablo A. Iglesias ()
Additional contact information
Tatsat Banerjee: Johns Hopkins University
Satomi Matsuoka: RIKEN Center for Biosystems Dynamics Research
Debojyoti Biswas: Johns Hopkins University
Yuchuan Miao: Johns Hopkins University
Dhiman Sankar Pal: Johns Hopkins University
Yoichiro Kamimura: RIKEN Center for Biosystems Dynamics Research
Masahiro Ueda: RIKEN Center for Biosystems Dynamics Research
Peter N. Devreotes: Johns Hopkins University
Pablo A. Iglesias: Johns Hopkins University
Nature Communications, 2023, vol. 14, issue 1, 1-24
Abstract:
Abstract The plasma membrane is widely regarded as the hub of the numerous signal transduction activities. Yet, the fundamental biophysical mechanisms that spatiotemporally compartmentalize different classes of membrane proteins remain unclear. Using multimodal live-cell imaging, here we first show that several lipid-anchored membrane proteins are consistently depleted from the membrane regions where the Ras/PI3K/Akt/F-actin network is activated. The dynamic polarization of these proteins does not depend upon the F-actin-based cytoskeletal structures, recurring shuttling between membrane and cytosol, or directed vesicular trafficking. Photoconversion microscopy and single-molecule measurements demonstrate that these lipid-anchored molecules have substantially dissimilar diffusion profiles in different regions of the membrane which enable their selective segregation. When these diffusion coefficients are incorporated into an excitable network-based stochastic reaction-diffusion model, simulations reveal that the altered affinity mediated selective partitioning is sufficient to drive familiar propagating wave patterns. Furthermore, normally uniform integral and lipid-anchored membrane proteins partition successfully when membrane domain-specific peptides are optogenetically recruited to them. We propose “dynamic partitioning” as a new mechanism that can account for large-scale compartmentalization of a wide array of lipid-anchored and integral membrane proteins during various physiological processes where membrane polarizes.
Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/s41467-023-43615-2 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43615-2
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-023-43615-2
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().