Matthieu Sainlos

ALPINE enables 3D single-molecule imaging and tracking of endogenous proteins in native environments with high resolution and dynamic quantification.

This study identifies Dvl2 as a novel component of the axon initial segment (AIS) and reveals its role in AIS assembly through MTCL1-dependent microtubule recruitment.

This study uses synchrotron XRF imaging to show manganese accumulates in the Golgi and postsynapses of neurons and astrocytes, with astrocytes taking up more manganese and reducing neuronal uptake.

The paper shows that βII and βIII spectrin paralogues form a dual system in the dendritic MPS, with structural redundancy and paralogue-specific regulation.

The paper develops a nanobody-gold conjugate for dual light-electron microscopy to label GFP-tagged synaptic proteins with high specificity and nanoscale resolution.

The paper develops paralog-specific intrabodies for PSD-93 and SAP102 to study excitatory synapse organization.

The paper investigates how AMPAR surface diffusion and desensitization contribute to frequency-dependent synaptic adaptation during high-frequency stimulation.

This study measures the binding kinetics of synaptic ligand-receptor interactions using a micropatterned cellular model and identifies differences in binding regimes between SynCAM1 and Nrx1β-Nlg1 complexes.

The paper develops synthetic binders specific to PSD-95 for imaging endogenous proteins with minimal impact on function and compatibility with super-resolution techniques.

This study uses a knock-in mouse model to monitor and manipulate AMPA receptor mobility, showing its role in synaptic plasticity and memory formation.

The paper shows MDGAs delay excitatory synapse development by altering neuroligin behavior through fast diffusion and reduced mobility.

This study shows that impaired AMPA receptor surface diffusion contributes to synaptic plasticity and memory deficits in Huntington’s disease, and that tianeptine can restore these functions.

The paper shows that neuroligin-1 alignment with AMPA receptor nanodomains is critical for synaptic transmission efficiency, as disrupting this alignment reduces transmission.