Interaction between an Integral Protein of the Nuclear Envelope Inner Membrane and Human Chromodomain Proteins Homologous to HP1

作者：Qian Ye, Howard J. Worman · 发表于：Journal of Biological Chemistry · 年份：1996 · DOI：10.1074/jbc.271.25.14653 · 被引用次数：410 · 研究领域：Nuclear Structure and Function、Genomics and Chromatin Dynamics、RNA Research and Splicing

At the nuclear envelope in higher eukaryotic cells, the nuclear lamina and the heterochromatin are adjacent to the inner nuclear membrane, and their attachment is presumably mediated by integral membrane proteins. In a yeast two-hybrid screen, the nucleoplasmic domain of lamin B receptor (LBR), an integral protein of the inner nuclear membrane, associated with two human polypeptides homologous to Drosophila HP1, a heterochromatin protein involved in position-effect variegation. LBR fusion proteins bound to HP1 proteins synthesized by in vitro translation and present in cell lysates. Antibodies against LBR also co-immunoprecipitated HP1 proteins from cell extracts. LBR can interact with chromodomain proteins that are highly conserved in eukaryotic species and may function in the attachment of heterochromatin to the inner nuclear membrane in cells.