Travelling Chemotactic Aggregates at Mesoscopic Scale and BiStability

International audienceWe investigate numerically a model consisting in a kinetic equation for the biased motion of bacteria following a run-and-tumble process, coupled with two reaction-diffusion equations for chemical signals. This model exhibits asymptotic propagation at a constant speed. In particular, it admits travelling wave solutions. To capture this propagation, we propose a well-balanced numerical scheme based on Case's elementary solutions for the kinetic equation, and L-splines for the parabolic equations. We use this scheme to explore the Cauchy problem for various parameters. Some examples far from the diffusive regime lead to the coexistence of two waves travelling at different speeds. Numerical tests support the hypothesis that they are both locally asymptotically stable. Interestingly, the exploration of the bifurcation diagram raises counter-intuitive features

Psr1p interacts with SUN/sad1p and EB1/mal3p to establish the bipolar spindle

Regular Abstracts - Sunday Poster Presentations: no. 382During mitosis, interpolar microtubules from two spindle pole bodies (SPBs) interdigitate to create an antiparallel microtubule array for accommodating numerous regulatory proteins. Among these proteins, the kinesin-5 cut7p/Eg5 is the key player responsible for sliding apart antiparallel microtubules and thus helps in establishing the bipolar spindle. At the onset of mitosis, two SPBs are adjacent to one another with most microtubules running nearly parallel toward the nuclear envelope, creating an unfavorable microtubule configuration for the kinesin-5 kinesins. Therefore, how the cell organizes the antiparallel microtubule array in the first place at mitotic onset remains enigmatic. Here, we show that a novel protein psrp1p localizes to the SPB and plays a key role in organizing the antiparallel microtubule array. The absence of psr1+ leads to a transient monopolar spindle and massive chromosome loss. Further functional characterization demonstrates that psr1p is recruited to the SPB through interaction with the conserved SUN protein sad1p and that psr1p physically interacts with the conserved microtubule plus tip protein mal3p/EB1. These results suggest a model that psr1p serves as a linking protein between sad1p/SUN and mal3p/EB1 to allow microtubule plus ends to be coupled to the SPBs for organization of an antiparallel microtubule array. Thus, we conclude that psr1p is involved in organizing the antiparallel microtubule array in the first place at mitosis onset by interaction with SUN/sad1p and EB1/mal3p, thereby establishing the bipolar spindle.postprin