Update and Potential Opportunities in CBP [Cyclic Adenosine Monophosphate (cAMP) Response Element-Binding Protein (CREB)-Binding Protein] Research Using Computational Techniques

Oluwayimika E Akinsiku,Opeyemi S Soremekun,Mahmoud E S Soliman

doi:10.1007/s10930-020-09951-8

Abstract

CBP [cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB)-binding protein] is one of the most researched proteins for its therapeutic function. Several studies have identified its vast functions and interactions with other transcription factors to initiate cellular signals of survival. In cancer and other diseases such as Alzheimer’s, Rubinstein-taybi syndrome, and inflammatory diseases, CBP has been implicated and hence an attractive target in drug design and development. In this review, we explore the various computational techniques that have been used in CBP research, furthermore we identified computational gaps that could be explored to facilitate the development of highly therapeutic CBP inhibitors.

Highlights

The CAMP responsive element-binding (CREB) (cyclic adenosine monophosphate response element-binding protein) Binding Protein (CBP), is a protein encoded by the CREBBP gene
The histone acetyltransferase (HATs) domain, part of the CREB binding protein is necessary for protein–protein interactions, histone and non-histone alike such as NCOA3 and FOXO1
Since mutant KRAS drives the activation of CAMP responsive element-binding (CREB), it is only appropriate to devise an inhibitor that can effectively do such through RAF/MEK/ERK signalling pathway inducing apoptosis in cancer cells [40]

Summary

Introduction

The CREB (cyclic adenosine monophosphate (cAMP) response element-binding protein) Binding Protein (CBP), is a protein encoded by the CREBBP gene. CBP is a bromodomain-containing protein which emphasises its functionality in identifying acetylated lysine in histone proteins while acting as effectors in signal associated with acetylation [1]. This class of protein has been reported to play a significant role in many biological and physiological processes, including transcription, differentiation, and apoptosis, whose activity is regulated by phosphorylation [1]. The histone acetyltransferase (HATs) domain, part of the CREB binding protein is necessary for protein–protein interactions, histone and non-histone alike such as NCOA3 and FOXO1. In 1993, p300, a Switch/ Sucrose Non-Fermentable (SWI/SNF) complexes binding protein family was identified.

Bromodomain

Various Attempt to Target CBP

Results

Computer‐Aided Techniques in Studies of CREB‐Binding Protein

Findings

Conclusion