Past Seminars

Here is the list of our past seminars :


Jonas Ranft (LPS, ENS, Paris). Biophysics Seminar ENS-ESPCI

Friday 20 October 2017 13:00-14:00 - ESPCI, Amphi Joliot, 2nd Floor, Staircase N

Lifetime of a structure evolving by cluster aggregation and particle loss, and application to postsynaptic scaffold domains

The aggregation of proteins in the cell membrane plays an important role in the formation of mesoscopic biological structures such as E-cadherin clusters or postsynaptic scaffold domains in neurons. Focussing on the case of inhibitory synapse components, we proposed a model for the formation and size determination of postsynaptic scaffold domains, explaining the observed domain sizes of scaffold clusters by a dynamic balance between the aggregation of scaffold proteins diffusing while bound to glycine receptors at the neuron membrane and scaffold protein turnover [1]. Out-of-equilibrium fluctuations due to stochastic aggregation and particle removal affect the stability of the formed structures, and one may ask what is the typical timescale during which they persist. Here, we calculate the characteristic lifetime of such structures formed by aggregation and removal, and discuss implications for the stability of inhibitory postsynaptic scaffold domains.

[1] Ranft, J., Almeida, L. G., Rodriguez, P. C., Triller, A., & Hakim, V. (2017). An aggregation-removal model for the formation and size determination of post-synaptic scaffold domains. PLoS Computational Biology, 13(4), e1005516–18. http://doi.org/10.1371/journal.pcbi.1005516






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Jonas Ranft (LPS, ENS, Paris). Biophysics Seminar ENS-ESPCI

Friday 20 October 2017 13:00-14:00 - ESPCI, Amphi Joliot, 2nd Floor, Staircase N

Lifetime of a structure evolving by cluster aggregation and particle loss, and application to postsynaptic scaffold domains

The aggregation of proteins in the cell membrane plays an important role in the formation of mesoscopic biological structures such as E-cadherin clusters or postsynaptic scaffold domains in neurons. Focussing on the case of inhibitory synapse components, we proposed a model for the formation and size determination of postsynaptic scaffold domains, explaining the observed domain sizes of scaffold clusters by a dynamic balance between the aggregation of scaffold proteins diffusing while bound to glycine receptors at the neuron membrane and scaffold protein turnover [1]. Out-of-equilibrium fluctuations due to stochastic aggregation and particle removal affect the stability of the formed structures, and one may ask what is the typical timescale during which they persist. Here, we calculate the characteristic lifetime of such structures formed by aggregation and removal, and discuss implications for the stability of inhibitory postsynaptic scaffold domains.

[1] Ranft, J., Almeida, L. G., Rodriguez, P. C., Triller, A., & Hakim, V. (2017). An aggregation-removal model for the formation and size determination of post-synaptic scaffold domains. PLoS Computational Biology, 13(4), e1005516–18. http://doi.org/10.1371/journal.pcbi.1005516






Archives des anciens séminaires  (42)


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