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C 末端结合:14-3-3 蛋白的功能扩展与作用机制

C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

作者信息

Coblitz Brian, Wu Meng, Shikano Sojin, Li Min

机构信息

Department of Neuroscience and High Throughput Biology Center, School of Medicine, Johns Hopkins University, 733 North Broadway, Baltimore, MD 21205, USA.

出版信息

FEBS Lett. 2006 Mar 6;580(6):1531-5. doi: 10.1016/j.febslet.2006.02.014. Epub 2006 Feb 17.

Abstract

Amino and carboxyl termini are unique positions in a polypeptide. They tend to be exposed in folded three dimensional structures. Diversity and functional significance of C-terminal sequences have been appreciated from studies of PDZ and PEX domains. Signaling 14-3-3 protein signaling by recognizing phosphorylated peptides plays a critical role in a variety of biological processes, including oncogenesis. The preferential binding of 14-3-3 to phosphorylated C-terminal sequences, mode III, provides a means of regulated binding and considerably expands the substrate repertoire of 14-3-3 interaction partners.

摘要

氨基端和羧基端是多肽中的独特位置。它们往往在折叠的三维结构中暴露。通过对PDZ和PEX结构域的研究,人们已经认识到C端序列的多样性和功能意义。14-3-3蛋白通过识别磷酸化肽段进行信号传导,在包括肿瘤发生在内的多种生物学过程中起关键作用。14-3-3与磷酸化C端序列的优先结合(模式III)提供了一种调节结合的方式,并大大扩展了14-3-3相互作用伙伴的底物范围。

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