Institute of Experimental Biochemistry II, University Clinic Wuerzburg, 97080 Wuerzburg, Germany.
Department of Cell and Cancer Biology, College of Medicine and Life Sciences, University of Toledo, MS 1010, Toledo, OH 43614, USA.
Cells. 2022 Nov 29;11(23):3817. doi: 10.3390/cells11233817.
LIM and SH3 protein 1 was originally identified as a structural cytoskeletal protein with scaffolding function. However, recent data suggest additional roles in cell signaling and gene expression, especially in tumor cells. These novel functions are primarily regulated by the site-specific phosphorylation of LASP1. This review will focus on specific phosphorylation-dependent interaction between LASP1 and cellular proteins that orchestrate primary tumor progression and metastasis. More specifically, we will describe the role of LASP1 in chemokine receptor, and PI3K/AKT signaling. We outline the nuclear role for LASP1 in terms of epigenetics and transcriptional regulation and modulation of oncogenic mRNA translation. Finally, newly identified roles for the cytoskeletal function of LASP1 next to its known canonical F-actin binding properties are included.
LIM 和 SH3 蛋白 1 最初被鉴定为具有支架功能的结构细胞骨架蛋白。然而,最近的数据表明其在细胞信号转导和基因表达中具有额外的作用,尤其是在肿瘤细胞中。这些新功能主要受到 LASP1 位点特异性磷酸化的调节。本综述将重点关注 LASP1 与细胞蛋白之间特定的磷酸化依赖性相互作用,这些相互作用协调原发性肿瘤的进展和转移。更具体地说,我们将描述 LASP1 在趋化因子受体和 PI3K/AKT 信号转导中的作用。我们将 LASP1 的核作用描述为表观遗传学和转录调节以及致癌 mRNA 翻译的调节。最后,还包括了 LASP1 除了其已知的经典 F-actin 结合特性之外的细胞骨架功能的新作用。