ArticleThe Journal of biological chemistry2008
Structural basis for CD44 recognition by ERM proteins.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 127 citations in OpenAlex.
- Article
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- The variational modulus density theory explains mechanical responses of cell membranes and membrane crosslinkers.Scientific reports · 2025Article
- New Bioinformatic Insight into CD44: Classification of Human Variants and Structural Analysis of CD44 Targeting.International journal of molecular sciences · 2025Article
- CD44 as a Central Integrator of Inflammation and Fibrosis: From Molecular Signaling to Environmental Modulation.International journal of molecular sciences · 2025Review
- Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.International journal of molecular sciences · 2024Article
- A bipartite NLS motif mediates the nuclear import ofFrontiers in cell and developmental biology · 2024Article
- Molecular basis of PIP2-dependent conformational switching of phosphorylated CD44 in binding FERM.Biophysical journal · 2023Article
- Cross-Linking Mass Spectrometry on P-Glycoprotein.International journal of molecular sciences · 2023Article
- Elucidation of Short Linear Motif-Based Interactions of the FERM Domains of Ezrin, Radixin, Moesin, and Merlin.Biochemistry · 2023Article
- The genetic landscape and possible therapeutics of neurofibromatosis type 2.Cancer cell international · 2023Review
- ConFERMing the role of talin in integrin activation and mechanosignaling.Journal of cell science · 2023Article
- Hyaluronan and Reactive Oxygen Species Signaling-Novel Cues from the Matrix?Antioxidants (Basel, Switzerland) · 2023Review
- Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023Review
- Hyaluronan Receptors as Mediators and Modulators of the Tumor Microenvironment.Advanced healthcare materials · 2023Review
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- Dysregulation and chronicity of pathogenic T cell responses in the pre-diseased stage of lupus.Frontiers in immunology · 2022Review
- High FRMD3 expression is prognostic for worse survival in rectal cancer patients treated with CCRT.International journal of clinical oncology · 2021Article
- Hyaluronan and Its Receptors as Regulatory Molecules of the Endothelial Interface.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021Review
- Structural analysis of the LDL receptor-interacting FERM domain in the E3 ubiquitin ligase IDOL reveals an obscured substrate-binding site.The Journal of biological chemistry · 2020Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CD44 is an important adhesion molecule that functions as the major hyaluronan receptor which mediates cell adhesion and migration in a variety of physiological and pathological processes. Although full activity of CD44 requires binding to ERM (ezrin/radixin/moesin) proteins, the CD44 cytoplasmic region, consisting of 72 amino acid residues, lacks the Motif-1 consensus sequence for ERM binding found in intercellular adhesion molecule (ICAM)-2 and other adhesion molecules of the immunoglobulin superfamily. Ultracentrifugation sedimentation studies and circular dichroism measurements revealed an extended monomeric form of the cytoplasmic peptide in solution. The crystal structure of the radixin FERM domain complexed with a CD44 cytoplasmic peptide reveals that the KKKLVIN sequence of the peptide forms a beta strand followed by a short loop structure that binds subdomain C of the FERM domain. Like Motif-1 binding, the CD44 beta strand binds the shallow groove between strand beta5C and helix alpha1C and augments the beta sheet beta5C-beta7C from subdomain C. Two hydrophobic CD44 residues, Leu and Ile, are docked into a hydrophobic pocket with the formation of hydrogen bonds between Asn of the CD44 short loop and loop beta4C-beta5C from subdomain C. This binding mode resembles that of NEP (neutral endopeptidase 24.11) rather than ICAM-2. Our results reveal a characteristic versatility of peptide recognition by the FERM domains from ERM proteins, suggest a possible mechanism by which the CD44 tail is released from the cytoskeleton for nuclear translocation by regulated intramembrane proteolysis, and provide a structural basis for Smad1 interactions with activated CD44 bound to ERM protein.
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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.