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As a family member of receptor tyrosine kinases, mesenchymal-epithelial transition receptor (Met) promotes cell proliferation and tumor metastasis by binding to growth factors to form specific dimers. The sensitive and efficient detection of Met dimerization and monomerization is essential in medical diagnosis and intervention. Herein, we proposed a visual method for Met dimerization by using a single stranded DNA named Met-Apt-G4 (MA), which contains a Met aptamer and G-quadruplex precursor sequences. Upon Met dimerization, the close proximity of two symmetric MAs allows the formation of G-quadruplex, which can induce chromogenic reaction in the presence of hemin. Furthermore, we demonstrated the transformation of MA and palindromic sequences capped tripodal DNA assembly to DNA coacervates (MA-DNA-NC). MA-DNA-NC may exert repulsion forces after binding to Met on cellular membrane, which caused the inhibition of Met dimerization. Moreover, MA-DNA-NC can effectively inhibit cellular cytoskeleton reorganization, which may eventually interfere with cell migration. This strategy may pave a new pathway to develop DNA coacervates based regulation of cellular migration.
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http://dx.doi.org/10.1016/j.jcis.2025.138718 | DOI Listing |
J Phys Chem B
September 2025
Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States.
The accurate simulation of realistic biomembranes is a long-term goal in the field of membrane biophysics. Efforts to simulate increasingly complex lipid bilayers, consisting of multiple lipid types and proteins, have been hindered by the shortcomings of current force fields, both coarse-grained and all-atom, in the modeling of protein-protein and protein-lipid interactions. Due to the fundamental importance of protein dimerization to cellular signaling and protein trafficking, the study of protein-protein association and the related dimerization free energies has received significant attention in both simulations and experiments.
View Article and Find Full Text PDFNat Commun
September 2025
Laboratory of Molecular Genetics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD, USA.
Stereocilia are F-actin-based cylindrical protrusions on the apical surface of inner ear hair cells that function as biological mechanosensors of sound and acceleration. During stereocilia development, specific unconventional myosins transport proteins and phospholipids as cargo and mediate elongation, differentiation and acquisition of the mechanoelectrical transduction (MET). How unconventional myosins localize themselves and cargo in stereocilia using energy from ATP hydrolysis is only partially understood.
View Article and Find Full Text PDFJ Colloid Interface Sci
August 2025
State Key Laboratory of Digital Medical Engineering, School of Biological Science and Medical Engineering, Southeast University, Nanjing 210096, PR China. Electronic address:
As a family member of receptor tyrosine kinases, mesenchymal-epithelial transition receptor (Met) promotes cell proliferation and tumor metastasis by binding to growth factors to form specific dimers. The sensitive and efficient detection of Met dimerization and monomerization is essential in medical diagnosis and intervention. Herein, we proposed a visual method for Met dimerization by using a single stranded DNA named Met-Apt-G4 (MA), which contains a Met aptamer and G-quadruplex precursor sequences.
View Article and Find Full Text PDFLung Cancer (Auckl)
August 2025
Department of Pulmonary and Critical Care Medicine, The Second Affiliated Hospital of Zhejiang Chinese Medical University, Hangzhou, Zhejiang, People's Republic of China.
Epidermal growth factor receptor kinase domain duplication (EGFR-KDD) is a rare form of EGFR mutation. Unlike the classical mutations such as exon 19 deletion and exon 21 p.L858R point mutation, EGFR-KDD is a special type of large genomic rearrangement (LGR) that results in the duplication of the tyrosine kinase domain at the protein level, leading to the formation of an intramolecular dimer and activation of the EGFR signaling pathway.
View Article and Find Full Text PDFJ Mol Biol
August 2025
Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia. Electronic address:
Apolipoprotein A-I (apoA-I) plays important roles in clearing cholesterol and phospholipids from peripheral tissues, forming high-density lipoprotein (HDL). However, despite this important function, apoA-I has a propensity to form amyloid fibrils implicated in atherosclerosis and hereditary amyloidosis. Historically, structural determination of lipid-free or lipid-poor apoA-I has been difficult.
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