Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10758356 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
The WASP family of proteins has emerged as important regulators that connect multiple signaling pathways to regulate the actin cytoskeleton. Dictyostelium cells express WASP, as well as a WASP related protein, WASP-B, endoded by wasB gene. WASP-B contains many of the domains present in WASP. Analysis of wild type, wasB null cells revealed that WASP-B is required for proper control of F-actin polymerization in response to a cAMP gradient. Due to the lack of tight control on actin polymerization, wasB null cells exhibited higher level of F-actin polymerization. wasBâ cells extend more de novo pseudopods laterally and their average life span is longer than those of wild type cells, causing more turns and inefficient chemotaxis. YFP-WASP-B appears to be uniformly distributed in the cytosol and shows no translocation to cortical membrane upon cAMP stimulation. Active RacC pull-down assay reveals that the level of active RacC in wasBâ cells is significantly higher than wild type cells. Moreover, the distribution of active RacC is not localized in wasBâ cells. We conclude that chemotaxis defects of wasBâ cells are likely to result from the aberrant regulation of RacC activation and localization.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Chang Y. Chung, Alexander Feoktistov, Ryan J. Hollingsworth, Francisco Rivero, Nicole S. Mandel,