ArticleBiophysical journal2022
Molecular mechanism of CD44 homodimerization modulated by palmitoylation and membrane environments.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Diverse ancestral myosin motors generate and segregate distinct types of nanocluster-rich domains at the plasma membrane.Science advances · 2026Article
- Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors.Cell communication and signaling : CCS · 2026Review
- Regulation of TMEM2-mediated hyaluronan degradation by CD44 and LYVE-1.Frontiers in molecular biosciences · 2026Article
- Photoaffinity Labeling Reveals a Role for the Unusual Triply Acylated PhospholipidJournal of the American Chemical Society · 2025Article
- CD44 facilitates adhesive interactions in airineme-mediated intercellular signaling.bioRxiv : the preprint server for biology · 2025Article
- CD44 facilitates adhesive interactions in airineme-mediated intercellular signaling.Frontiers in cell and developmental biology · 2025Article
- The cell adhesion molecule CD44 acts as a modulator of 5-HT7 receptor functions.Cell communication and signaling : CCS · 2024Article
- Biophysics of protein-lipid interactions.Biophysical journal · 2024Article
- CD44: a cancer stem cell marker and therapeutic target in leukemia treatment.Frontiers in immunology · 2024Review
- Molecular basis of PIP2-dependent conformational switching of phosphorylated CD44 in binding FERM.Biophysical journal · 2023Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The homodimerization of CD44 plays a key role in an intercellular-to-extracellular signal transduction and tumor progression. Acylated modification and specific membrane environments have been reported to mediate translocation and oligomerization of CD44; however, the underlying molecular mechanism remains elusive. In this study, extensive molecular dynamics simulations are performed to characterize the dimerization of palmitoylated CD44 variants in different bilayer environments. CD44 forms homodimer depending on the cysteines on the juxta-membrane domains, and the dimerization efficiency and packing configurations are defected by their palmitoylated modifications. In the phase-segregated (raft included) membrane, homodimerization of the palmitoylated CD44 is hardly observed, whereas PIP2 addition compensates to realize dimerization. However, the structure of CD44 homodimer formed in the phase-segregated bilayer turns susceptive and PIP2 addition allows for an extensive conformation of the cytoplasmic domain, a proposal prerequisite to access the cytoskeleton linker proteins. The results unravel a delicate competitive relationship between PIP2, lipid raft, and palmitoylation in mediating protein homodimerization, which helps to clarify the dynamic dimer conformations and involved cellular signaling of the CD44 likewise proteins.
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