Nuclear lamina assembly, synthesis and disaggregation during the cell cycle in synchronized HeLa cells

作者：Erich Jost, Robert T. Johnson · 发表于：Journal of Cell Science · 年份：1981 · DOI：10.1242/jcs.47.1.25 · 被引用次数：65 · 研究领域：Nuclear Structure and Function、Genomics and Chromatin Dynamics、Skin and Cellular Biology Research

ABSTRACT The pattern of assembly, synthesis and disaggregation of the nuclear envelope-associated lamina in synchronized HeLa cells has been examined by means of immunofluorescence microscopy of cell preparations treated with antibody to lamina polypeptide LP67 or lamin B, using the nomenclature of Gerace and Blobel. During the cell cycle the distribution of lamina polypeptide varies dramatically. Three distinct stages can be detected with respect to its location and synthesis: Lamina polypeptide is cytoplasmically distributed during cell division particularly at the time of complete nuclear envelope breakdown. At telophase it is reassembled and becomes associated with regions of the chromosome surface. This process continues into early G1, lamina polypeptide associating progressively with the outer surface of the chromosomes; simultaneously its cytoplasmic concentration is reduced. The traffic of antigen from cytoplasm to the chromosomes is highest between telophase and G1 but continues at a reduced rate during G1. Inhibition of protein synthesis during division and G1 does not inhibit G1 lamina reformation, suggesting that the G1 lamina is constructed from depolymerized cytoplasmically-stored polypeptide derived from the previous cell cycle.Lamin B is synthesized in S-phase. The protein is rapidly accumulated at the nuclear periphery during the doubling of the nuclear surface. There is very little if any cytoplasmic location of lamina polypeptide in S-phase cells. The S-pha...