2026年3月16日出版的《自然—细胞生物学》杂志发表了德国凯泽斯劳滕大学Tanja Maritzen团队的最新成果，他们的最新研究提出了果糖-1,6-二磷酸将糖酵解活性与细胞粘附结合。

通过全基因组筛选，该课题组人员鉴定出醛缩酶A，一种转化果糖-1,6-二磷酸（FBP）的关键糖酵解酶，作为一种将代谢通量与FA组装和细胞形态发生联系起来的调节开关。该课题组人员发现细胞FBP作为一种信号代谢物，将代谢细胞状态的信息传递给基于肌动蛋白的细胞粘附和突起机制。该机制涉及FBP与Rac1抑制剂RCC2结合，并伴随Rac1活性的升高，导致肌动蛋白重组、FA组装增加和突起活性升高。

在这里，研究组预测这种机制对从发育到癌症的过程至关重要。

据介绍，细胞粘附到细胞外基质是必不可少的形态发生，组织完整性和生存信号。最了解的粘连结构是局灶性粘连（FAs）。尽管它们很重要，但它们对将FA动力学与其他细胞过程（如代谢）相结合的上游因素的了解仍然是零碎的。

附：英文原文

Title: Fructose-1,6-bisphosphate couples glycolytic activity to cell adhesion

Author: Hoffmann, Lennart, Duchmann, Marlen, Lazarow, Katina, Huang, Yun-Hsuan, Lukas, Fabian, Lo, Wen-Ting, Feil, Regina, Schmied, Christopher, Lehmann, Martin, Lunn, John E., Piazza, Ilaria, von Kries, Jens P., Haucke, Volker, Maritzen, Tanja

Issue&Volume: 2026-03-16

Abstract: Cellular adhesion to the extracellular matrix is essential for morphogenesis, tissue integrity and survival signalling. The best understood adhesion structures are focal adhesions (FAs). In spite of their importance, our knowledge of upstream factors that integrate FA dynamics with other cellular processes, such as metabolism, remains fragmentary. Using a genome-wide screen, we identify aldolase A, a key glycolytic enzyme that converts fructose-1,6-bisphosphate (FBP), as a regulatory switch that links metabolic flux to FA assembly and cell morphogenesis. We show that cellular FBP serves as a signalling metabolite, which transmits information about the metabolic cell state to the actin-based machinery for cell adhesion and protrusion. This mechanism involves FBP binding to the Rac1 inhibitor RCC2 and a concomitant elevation of Rac1 activity resulting in actin reorganization, increased FA assembly and elevated protrusive activity. Here we predict this mechanism to be crucial for processes ranging from development to cancer.

DOI: 10.1038/s41556-026-01911-1

Source: https://www.nature.com/articles/s41556-026-01911-1