Rana A P, Ruff P, Maalouf G J, Speicher D W, Chishti A H
Department of Biomedical Research, St. Elizabeth's Hospital, Tufts University School of Medicine, Boston, MA 02135.
Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6651-5. doi: 10.1073/pnas.90.14.6651.
Dematin is an actin-bundling protein originally identified in the human erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by the cAMP-dependent protein kinase and is restored after dephosphorylation. Here we report the complete primary structure of human erythroid dematin, whose sequence includes a homologue of the "headpiece" sequence found at the C terminus of villin. This headpiece is essential for villin function in inducing microvillar development and actin redistribution. The widespread expression of dematin transcripts in human tissues suggests that dematin and its homologues may substitute for villin in villin-negative tissues to regulate actin reorganization by a phosphorylation-regulated mechanism.
肌动蛋白结合蛋白最初是在人类红细胞膜骨架中发现的。其肌动蛋白结合活性在被环磷酸腺苷依赖性蛋白激酶磷酸化后丧失，并在去磷酸化后恢复。我们在此报道人类红细胞肌动蛋白结合蛋白的完整一级结构，其序列包含在绒毛蛋白C末端发现的“头部”序列的同源物。该头部对于绒毛蛋白在诱导微绒毛发育和肌动蛋白重新分布中的功能至关重要。肌动蛋白结合蛋白转录本在人类组织中的广泛表达表明，肌动蛋白结合蛋白及其同源物可能在绒毛蛋白阴性组织中替代绒毛蛋白，通过磷酸化调节机制来调节肌动蛋白重组。
