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 Mammalian Abp1 may function at the interface of endocytosis and the actin cytoskeleton in both pre- and postsynapses

(Elavarasi Dharmalingam, Akvile Inciute, Dennis Koch)

Mammalian Abp1 is a multi-domain protein that encompasses two independently acting F-actin-binding modules (Kessels et al., 2000). Our results indicate that Abp1‘s function may be the integration of membrane trafficking and the actin cytoskeletal organization, a role that seems to be controlled by signaling pathways converging on Abp1 (Kessels et al., 2001; Figure 1).

Abp1 accumulates at the F-actin-rich leading edge and at sites of endocytosis.

Figure 1: Abp1 accumulates at the F-actin-rich leading edge and at sites of endocytosis. NIH 3t3 cells were stimulated with growth factors and immunostained for Abp1 (green) and dynamin (red). Abp1 accumulations were observed at the leading edge and also at punctate cortical sites immunopositive for dynamin (overlap of red and green appears yellow).

In close collaboration with Dr. Michael Kessels, this project tries to unravel the signaling pathways converging onto Abp1 and addresses the role of Abp1 functions in the modulation of signals originating from activated receptors.

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