کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2179076 | 1549766 | 2007 | 12 صفحه PDF | دانلود رایگان |

Cells accomplish the non-selective uptake of extracellular fluids, antigens and pathogens by the endocytic process of macropinocytosis. The protein SWAP-70 is a widely expressed, pleckstrin-homology (PH) domain-containing protein that marks a transitional subset of actin filaments in motile cells. Here we report that the protein SWAP-70 associates transiently with macropinosomes in dendritic cells and NIH/3T3 fibroblasts. The association of SWAP-70 with macropinosomes is preceded by the accumulation of Rac-GTP and followed by that of Rab5. Three regions of SWAP-70, the N-terminal region, the PH domain and the C-terminal region, contribute in a combinatorial manner to the transient association with newly formed macropinosomes in the cell periphery and occasionally with aged macropinosomes on their passage to the cell center. These data identify SWAP-70 as a transient component of early macropinosomes.
Journal: European Journal of Cell Biology - Volume 86, Issue 1, 17 January 2007, Pages 13–24