Members of the nebulin family regulate actin filament stability and function in muscle. The two smallest family members, Lasp1 and Lasp2, are also expressed in non-muscle tissues. Lasp1 is a multi-domain protein containing an N-terminal LIM domain, two actin-binding nebulin modules, a linker region, and a C-terminal SH3 domain. LIM domains are protein–protein interaction motifs composed of two zinc-coordinating modules (E. Butt und D. Raman, Front Oncol, 2018).

We recently demonstrated that Lasp1 is expressed at the slit diaphragm in podocytes and anchored to the actin cytoskeleton. Interestingly, Lasp1 interacts with the slit diaphragm protein CD2AP. CD2AP knockout results in a redistribution of LASP1 expression in podocytes. In collaboration with Prof. M. Krahn'sgroup, we showed that Lasp1 plays an important role in maintaining slit diaphragm integrity in nephrocytes (C. Lepa, FASEB J, 2020). In the coming years, we will investigate the role of Lasp1 in regulating actin cytoskeleton dynamics in podocytes, both in vitro and in vivo.