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In this study, we tested the hypothesis that Wiskott Aldrich Syndrome protein (WASp)-activated Arp2/3 and the mammalian
Diaphanous-related formin mDia1 actin assembly activities work in tandem to generate the essential cytoskeletal structures
required for T cell chemotaxis. Informed by studies of Drf1
mice (mDia1 knockout) generated in our lab, we bred mDia1
knockout with Wasp-targeted animals, postulating that combined mDia1 and WASp ablation would cumulatively impact T cell
chemotactic migration. For these experiments, splenic T cell migration in wild-type, Wasp
cells were tested. Wasp
T cells were mildly defective in migration when compared to the severe defect again observed
cells. However, the defect was cumulative in Drf1
T cells; interestingly, the Wasp knockout migratory defect
was compounded upon loss of a single Drf1 allele (Drf1
). Further, while Wasp
T cell ruffling on adhesive substrates
was comparable to that of wild-type cells, Drf1
T cells failed to ruffle at all. mDia1 and WASp complex in cells.
Upon ligation of CD3 and CD28 WASp and mDia1 co-immunoprecipitated and co-localized at the cell periphery within ruffles.
Additional experiments identified the shared WASp and mDia1 binding partner DIP/WISH as a linker. In vitro, loss of DIP
expression eliminated the WASp-mDia1 complex and blocked T cell migration. Collectively, these data identify a molecular
mechanism for collaboration between branching and non-branched actin assembly activities in T cell function.
Alberts earned BA and PhD degrees from the University of California, San Diego (1983-1993). He was a Post-Doctoral Fellow at the Imperial Cancer Research and the University of California, San Franscisco (1994-1999). In 2000, Alberts joined the Van Andel Research Institute as a Scientific Investigator and Head of the Laboratory of Cell Structure & Signal Integration. He was promoted to Senior Scientific Investigator in 2006 and then to Distinguished Scientific Investigator and Professor of Cancer and Cell Biology in 2009.
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