The nuclear architectural protein HMGA1a triggers receptor-mediated endocytosis.
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| Abstract |
High mobility group proteins A (HMGA), nuclear architectural factors, locate in the cell nuclei and mostly execute gene-regulation function. However, our results reveal that a HMGA member (HMGA1a) has a unique plasma membrane receptor; this receptor specifically binds to HMGA-decorated species, effectively mediates endocytosis, and internalizes extracellular HMGA-functionalized cargoes. Indeed, dyes or nanoparticles labeled with HMGA1a protein readily enter Hela cells. Using a stratagem chemical cross-linker, we covalently bonded the HMGA receptor to the HMGA1a-GFP fusion protein, thus capturing the plasma membrane receptor. Subsequent Western blots and SDS-PAGE gel revealed that the HMGA receptor is a 26-kDa protein. Confocal live-cell microscopic imaging was used to monitor the whole endocytic process, in which the internalized HMGA1a-decorated species are transported by motor proteins on microtubules and eventually arrive at the late endosomes/lysosomes. Cell viability assays also suggested that extracellular HMGA1a protein directly influences the survival ability of Hela cells in a dose-dependent manner, implying versatility of HMGA1a protein and its potent role to suppress cancer cell survivability and to regulate growth.
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| Authors | Wuwei Wu, Wei Wan, Alexander D Q Li |
| Journal | Journal of cellular biochemistry (J Cell Biochem) Vol. 108 Issue 4 Pg. 791-801 (Nov 01 2009) ISSN: 1097-4644 [Electronic] United States |
| PMID | 19739099 (Publication Type: Journal Article, Research Support, N.I.H., Extramural) |
| Copyright | (c) 2009 Wiley-Liss, Inc. |
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