Phosphorylation of Nck

人体由各种组织组成，这些组织由具有专门功能的不同类型的细胞组成。人类细胞功能的协调调节涉及介导细胞蛋白活性修饰的生化过程。在这些影响蛋白质活性的修饰中，磷酸化是至关重要的，其特征在于通过被定义为蛋白激酶的专门酶将磷酸基团转移到特定氨基酸上。我们的实验室感兴趣的是对蛋白质磷酸化功能的基本理解和参与这一过程的蛋白激酶的鉴定。作为一个工作模型，我们调查的小蛋白NCK（非催化区的酪氨酸激酶），我们发现磷酸化在各种应力条件下已知激活的蛋白激酶的子集。总之，我们的工作旨在确定Nck磷酸化位点，并确定Nck磷酸化如何影响其细胞定位，与其他蛋白质的相互作用和生物学功能。我们坚信，我们对蛋白质磷酸化的研究将通过提供对调节关键细胞功能的基本机制的详细了解而使整个科学界受益。

The human body is composed of various tissues, which consist of different types of cells with specialized functions. Coordinated regulation of the human cell functions involves biochemical processes mediating modifications of cellular proteins activity. Among these modifications that affect proteins activities, phosphorylation, characterized by the transfer of a phosphate group on specific amino acids by specialized enzymes defined as protein kinases, is critical. Our laboratory is interested in the basic understanding of the function of protein phosphorylation and the identification of protein kinases participating in this process. As a working model, we investigate the small protein Nck (non catalytic-region of tyrosine kinase), that we found phosphorylated in various stress conditions known to activate a subset of protein kinases. Overall, our work aims to identify Nck phosphorylated site(s) and to determine how phosphorylation of Nck impacts its cellular localization, interaction with other proteins and biological functions. We strongly believe that our research on protein phosphorylation will benefit the whole scientific community by providing a detailed understanding of fundamental mechanisms regulating crucial cell functions.