Biomedical subjects

Emilie Perret

Publications and source records attributed to Emilie Perret.

3 recordsLinked to original sources

PubMed2005

Evolving endosomes: how many varieties and why?

The cell biologist's insight into endosomal diversity, in terms of both form and function, has increased dramatically in the past few years. This understanding has been promoted by the availability of powerful new techniques that allow imaging of both cargo and machinery in the endocytic process in real time, and by our ability to inhibit components of this machinery by RNA interference. The emerging picture from these studies is of a highly complex, dynamic and adaptable endosomal system that interacts at various points with the secretory system of the cell.

Animals↗

PubMed2004

[Molecular aspects of cadherin-mediated cell adhesion: the first moments of the interaction].

Cadherins play a major role in the development and maintenance of all solid tissues. These transmembrane glycoproteins are responsible for calcium-dependent homophilic cell interactions. Recently, many different experimental approaches have been used to untangle the molecular basis of cadherin-mediated adherence. Various models have been suggested, particularly from high-resolution structures. Whilst the adherence mechanism is still under controversy, it is widely accepted that the specificity of the adherent interaction is localized to the N-terminal domain. New biophysical techniques together with biological approaches will allow a better understanding of how cadherins regulate cell-cell adherence. Integrating kinetics properties of cadherin interaction at the single molecule level has led to a greater understanding of cadherin molecular regulations.

Animals↗

PubMed2002

Fast dissociation kinetics between individual E-cadherin fragments revealed by flow chamber analysis.

E-cadherin is the predominant adhesion molecule of epithelia. The interaction between extracellular segments of E-cadherin in the membrane of opposing cells is homophilic and calcium dependent. Whereas it is widely accepted that the specificity of the adhesive interaction is localized to the N-terminal domain, the kinetics of the recognition process are unknown. We report the first quantitative data describing the dissociation kinetics of individual E-cadherin interactions. Aggregation assays indicate that the two outermost domains of E-cadherin (E/EC1-2) retain biological activity when chemically immobilized on glass beads. Cadherin fragment trans-interaction was analysed using a flow chamber technique. Transient tethers had first-order kinetics, suggesting a unimolecular interaction. The unstressed lifetime of individual E-cadherin interactions was as brief as 2 s. A fast off rate and the low tensile strength of the E-cadherin bond may be necessary to support the high selectivity and plasticity of epithelial cell interactions.

Animals↗