Conserved motifs in voltage sensing proteins.
- Author:
Chang-He WANG
1
;
Zhen-Li XIE
;
Jian-Wei LV
;
Zhi-Dan YU
;
Shu-Li SHAO
Author Information
1. College of Life Science, Agriculture and Forestry, Qiqihar University, Qiqihar 161006, China. changhecool@163.com
- Publication Type:Journal Article
- MeSH:
Arginine;
chemistry;
Aspartic Acid;
chemistry;
Cell Membrane;
physiology;
Conserved Sequence;
Ion Channel Gating;
Ion Channels;
chemistry;
Membrane Potentials;
Protein Structure, Tertiary
- From:
Acta Physiologica Sinica
2012;64(4):379-386
- CountryChina
- Language:Chinese
-
Abstract:
This paper was aimed to study conserved motifs of voltage sensing proteins (VSPs) and establish a voltage sensing model. All VSPs were collected from the Uniprot database using a comprehensive keyword search followed by manual curation, and the results indicated that there are only two types of known VSPs, voltage gated ion channels and voltage dependent phosphatases. All the VSPs have a common domain of four helical transmembrane segments (TMS, S1-S4), which constitute the voltage sensing module of the VSPs. The S1 segment was shown to be responsible for membrane targeting and insertion of these proteins, while S2-S4 segments, which can sense membrane potential, for protein properties. Conserved motifs/residues and their functional significance of each TMS were identified using profile-to-profile sequence alignments. Conserved motifs in these four segments are strikingly similar for all VSPs, especially, the conserved motif [RK]-X(2)-R-X(2)-R-X(2)-[RK] was presented in all the S4 segments, with positively charged arginine (R) alternating with two hydrophobic or uncharged residues. Movement of these arginines across the membrane electric field is the core mechanism by which the VSPs detect changes in membrane potential. The negatively charged aspartate (D) in the S3 segment is universally conserved in all the VSPs, suggesting that the aspartate residue may be involved in voltage sensing properties of VSPs as well as the electrostatic interactions with the positively charged residues in the S4 segment, which may enhance the thermodynamic stability of the S4 segments in plasma membrane.
