Abba promotes PDGF-mediated membrane ruffling through activation of the small GTPase Rac1.
作者： Datong Zheng , Shuqiong Niu , Dan Yu , Xiaoguo H. Zhan , Xianchun Zeng
DOI: 10.1016/J.BBRC.2010.09.087
关键词: RAC1 、 Immunoprecipitation 、 Cell biology 、 Membrane protein 、 Membrane ruffling 、 Cell membrane 、 Lamellipodium 、 Platelet-derived growth factor receptor 、 Biology 、 Small GTPase
摘要: Abba is a member of the I-BAR-domain protein family that characterized by convex-shaped membrane-binding motif. Overexpression GFP-tagged in murine fibroblasts potentiated PDGF-mediated formation membrane ruffles and lamellipodia. Immunofluorescent microscopy pull-down analysis revealed GFP-Abba colocalized with an active form Rac1 enhanced Rac GTPase activity response to PDGF stimulation. Further immunoprecipitation assays demonstrated bound both wild-type constitutively binding either forms was significantly upon On other hand, mutant deficient failed promote ruffling activation PDGF. However, cells overexpressing truncated carrying I-BAR domain alone displayed numerous filopodia-like microspikes manner independent growth factors. Also, Rac-binding not affected treatment. Our data indicates interaction between full-length implicated deformation subjected factor-mediated regulation through C-terminal sequence.
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