Regulation of Dopamine-Dependent Behaviors by G Protein-Coupled Receptor Kinases

Gurevich, Eugenia V.; Gainetdinov, Raul R.; Gurevich, Vsevolod V.

doi:10.1007/978-1-4939-3798-1_11

Cited by 1 publication

(1 citation statement)

References 193 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Coexisting with other biological macromolecules such as RNA, DNA, lipids, and glycans, proteins operate in limited available space. , Therefore, stringent regulation mechanisms are needed for proteins to perform their programmed biological functions and ensure well-orchestrated response to various external and internal events in the cell . Overexpressed, inappropriately localized, or hyperactive proteins due to regulation failure may result in deleterious consequences and diseases. − A prime example highlighting the importance of tight protein regulation is the transcriptional factor p53, whose deregulation could lead to tumor development . Thus, strict cellular and molecular control mechanisms of protein activities are key to providing overall cellular viability and functionality (Figure ).…”

Section: Introductionmentioning

confidence: 99%

How the Local Environment of Functional Sites Regulates Protein Function

2020

View full text Add to dashboard Cite

Proteins form complex biological machineries whose functions in the cell are highly regulated at both the cellular and molecular levels. Cellular regulation of protein functions involves differential gene expressions, post-translation modifications, and signaling cascades. Molecular regulation, on the other hand, involves tuning an optimal local protein environment for the functional site. Precisely how a protein achieves such an optimal environment around a given functional site is not well understood. Herein, by surveying the literature, we first summarize the various reported strategies used by certain proteins to ensure their correct functioning. We then formulate three key physicochemical factors for regulating a protein’s functional site, namely, (i) its immediate interactions, (ii) its solvent accessibility, and (iii) its conformational flexibility. We illustrate how these factors are applied to regulate the functions of free/metal-bound Cys and Zn sites in proteins.

show abstract