Thirty years of the HAP2/3/4/5 complex

2017 
Abstract Thirty years of study of the HAP complex have provided a pretty good picture of the complex components and put forward its original features. The HAP complex is a modular transcriptional activator in which the DNA-binding domain (composed of three proteins, Hap2p, Hap3p, and Hap5p) and the activation domain (one protein, Hap4p) are separated. I summarize what is known about these proteins and their assembly, and also examine the role of this key regulator. In addition to its well known action on mitochondrial biogenesis and function, it also plays, indirectly, additional roles on various other cellular functions, thus keeping the different pathways of the cell, well balanced. What is know of its regulation is also discussed as well as possible applications in biotechnology. However, many questions remain to be answered, especially concerning the regulation, modularity and evolution of the complex, which are discussed in the final section. This article is part of a Special Issue entitled: Nuclear Factor Y in Development and Disease, edited by Prof. Roberto Mantovani.
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