Caveolin-1 (CAV1) has long been implicated in cancer progression, and while widely accepted as an oncogenic protein, CAV1 also has tumor suppressor activity. CAV1 was first identified in an early study as the primary substrate of Src kinase, a potent oncoprotein, where its phosphorylation correlated with cellular transformation. Indeed, CAV1 phosphorylation on tyrosine-14 (Y14; pCAV1) has been associated with several cancer-associated processes such as focal adhesion dynamics, tumor cell migration and invasion, growth suppression, cancer cell metabolism, and mechanical and oxidative stress. Despite this, a clear understanding of the role of Y14-phosphorylated pCAV1 in cancer progression has not been thoroughly established. Here, we provide an overview of the role of Src-dependent phosphorylation of tumor cell CAV1 in cancer progression, focusing on pCAV1 in tumor cell migration, focal adhesion signaling and metabolism, and in the cancer cell response to stress pathways characteristic of the tumor microenvironment. We also discuss a model for Y14 phosphorylation regulation of CAV1 effector protein interactions via the caveolin scaffolding domain.

中文翻译：

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肿瘤细胞caveolin-1的酪氨酸磷酸化：对癌症进展的影响

Caveolin-1 (CAV1) 长期以来一直与癌症进展有关，虽然被广泛接受为致癌蛋白，但 CAV1 还具有肿瘤抑制活性。CAV1 在早期研究中首次被鉴定为 Src 激酶的主要底物，Src 激酶是一种有效的癌蛋白，其磷酸化与细胞转化相关。事实上，酪氨酸 14（Y14；pCAV1）上的 CAV1 磷酸化与多种癌症相关过程有关，例如粘着斑动力学、肿瘤细胞迁移和侵袭、生长抑制、癌细胞代谢以及机械和氧化应激。尽管如此，对 Y14 磷酸化 pCAV1 在癌症进展中的作用的清楚认识尚未完全确定。在这里，我们概述了肿瘤细胞 CAV1 的 Src 依赖性磷酸化在癌症进展中的作用，专注于 pCAV1 在肿瘤细胞迁移、粘着斑信号传导和代谢以及癌细胞对肿瘤微环境特征性应激途径的反应中。我们还讨论了通过小窝支架结构域对 CAV1 效应蛋白相互作用进行 Y14 磷酸化调节的模型。