RNA结合蛋白和糖蛋白在细胞表面形成结构域，用于细胞穿透肽的进入，这一成果由波士顿儿童医院Ryan A. Flynn课题组经过不懈努力而取得。2025年2月27日出版的《细胞》杂志发表了这项成果。

小组提供的证据表明，一组RNA结合蛋白（RBPs）存在于活细胞表面。这些细胞表面RBPs (csRBPs)精确地组织成定义明确的纳米细胞，富含多种RBPs和glycoRNAs，并且细胞外RNase添加可以破坏它们的聚集。这些glycoRNA-csRBP细胞进一步作为细胞穿透肽转录反式激活因子（TAT）的细胞表面相互作用位点。从细胞表面去除RNA，或TAT失去RNA结合活性，是TAT细胞内化的缺陷。总之，该课题组研究人员通过定位glycoRNA-csRBP测量仪作为细胞与细胞外环境之间通信的调节剂，提供了扩展细胞表面视野的证据。

据悉，细胞表面的组成和组织决定了细胞如何与环境相互作用。传统上，糖基化跨膜蛋白被认为是质膜外表面的主要成分。

附：英文原文

Title: RNA-binding proteins and glycoRNAs form domains on the cell surface for cell-penetrating peptide entry

Author: Jonathan Perr, Andreas Langen, Karim Almahayni, Gianluca Nestola, Peiyuan Chai, Charlotta G. Lebedenko, Regan F. Volk, Diego Detrés, Reese M. Caldwell, Malte Spiekermann, Helena Hemberger, Namita Bisaria, Toshihiko Aiba, Francisco J. Sánchez-Rivera, Konstantinos Tzelepis, Eliezer Calo, Leonhard Mckl, Balyn W. Zaro, Ryan A. Flynn

Issue&Volume: 2025-02-27

Abstract: The composition and organization of the cell surface determine how cells interact with their environment. Traditionally, glycosylated transmembrane proteins were thought to be the major constituents of the external surface of the plasma membrane. Here, we provide evidence that a group of RNA-binding proteins (RBPs) is present on the surface of living cells. These cell-surface RBPs (csRBPs) precisely organize into well-defined nanoclusters enriched for multiple RBPs and glycoRNAs, and their clustering can be disrupted by extracellular RNase addition. These glycoRNA-csRBP clusters further serve as sites of cell-surface interaction for the cell-penetrating peptide trans-activator of transcription (TAT). Removal of RNA from the cell surface, or loss of RNA-binding activity by TAT, causes defects in TAT cell internalization. Together, we provide evidence of an expanded view of the cell surface by positioning glycoRNA-csRBP clusters as a regulator of communication between cells and the extracellular environment.

DOI: 10.1016/j.cell.2025.01.040

Source: https://www.cell.com/cell/abstract/S0092-8674(25)00109-6