Role of α and β Transmembrane Domains in Integrin Clustering

Actuators

Amir Shamloo¹  Ashkan Golgoon¹  Ebrahim Ghafar Zadeh² 

[1] Department of Mechanical Engineering, Sharif University of Technology, Tehran, Iran; E-Mail:;Department of Electrical Engineering, York University, Toronto, M3J1P3, Canada

关键词: integrin;    molecular dynamics;    oligomerization;   

DOI  :  10.3390/act4040267

来源: mdpi

【 摘 要 】

Integrins are transmembrane proteins playing a crucial role in the mechanical signal transduction from the outside to the inside of a cell, and vice versa. Nevertheless, this signal transduction could not be implemented by a single protein. Rather, in order for integrins to be able to participate in signal transduction, they need to be activated and produce clusters first. As integrins consist of α- and β-subunits that are separate in the active state, studying both subunits separately is of a great importance, for, in the active state, the distance between α- and β-subunits is long enough that they do not influence one another significantly. Thus, this study aims to investigate the tendency of transmembrane domains of integrins to form homodimers. We used both Steered and MARTINI Coarse-grained molecular dynamics method to perform our simulations, mainly because of a better resolution and computational feasibility that each of these methods could provide to us. Using the Steered molecular dynamics method for α- and β-subunits, we found that the localized lipid packing prevented them from clustering. Nonetheless, the lipid packing phenomenon was found to be an artifact after investigating this process using a coarse grained (CG) model. Exploiting the coarse-grained molecular dynamics simulations, we found that α- and β-subunits tend to form a stable homo-dimer.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.