Department of Medical Protein Research, VIB, Ghent University, Faculty of Medicine and Health Sciences, Albert Baertsoenkaai 3, B-9000 Ghent, Belgium.
Biochem Biophys Res Commun. 2011 Mar 4;406(1):101-6. doi: 10.1016/j.bbrc.2011.02.002. Epub 2011 Feb 3.
Different structural conformations of actin have been identified in cells and shown to reside in distinct subcellular locations of cells. In this report, we describe the localization of actin on a cage-like structure in metaphase HEK 293T cells. Actin was detected with the anti-actin antibodies 1C7 and 2G2, but not with the anti-actin antibody C4. Actin contained in this structure is independent of microtubules and actin filaments, and colocalizes with vimentin. Taking advantage of intermediate filament collapse into a perinuclear dense mass of cables when microtubules are depolymerized, we were able to relocalize actin to such structures. We hypothesize that phosphorylation of intermediate filaments at mitosis entry triggers the recruitment of different actin conformations to mitotic intermediate filaments. Storage and partition of the nuclear actin and antiparallel "lower dimer" actin conformations between daughter cells possibly contribute to gene transcription and transient actin filament dynamics at G1 entry.
已经在细胞中鉴定出不同的肌动蛋白结构构象,并表明它们位于细胞的不同亚细胞位置。在本报告中,我们描述了肌动蛋白在中期 HEK 293T 细胞笼状结构上的定位。肌动蛋白用抗肌动蛋白抗体 1C7 和 2G2 检测,但不能用抗肌动蛋白抗体 C4 检测。该结构中包含的肌动蛋白与微管和肌动蛋白丝无关,与波形蛋白共定位。利用微管解聚时中间丝塌陷成核周密集电缆的优势,我们能够将肌动蛋白重新定位到这些结构上。我们假设有丝分裂进入时中间丝的磷酸化触发了不同肌动蛋白构象向有丝分裂中间丝的募集。核肌动蛋白和反平行“下二聚体”肌动蛋白构象在子细胞中的储存和分配可能有助于基因转录和 G1 进入时短暂的肌动蛋白丝动力学。