The Cytoskeleton and Its Regulation by Calcium and Protons.

Plant Physiol

Biology Department, University of Massachusetts, Amherst, Massachusetts 01003

Published: January 2016


Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Calcium and protons exert control over the formation and activity of the cytoskeleton, usually by modulating an associated motor protein or one that affects the structural organization of the polymer.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4704593PMC
http://dx.doi.org/10.1104/pp.15.01506DOI Listing

Publication Analysis

Top Keywords

calcium protons
8
cytoskeleton regulation
4
regulation calcium
4
protons calcium
4
protons exert
4
exert control
4
control formation
4
formation activity
4
activity cytoskeleton
4
cytoskeleton modulating
4

Similar Publications

The Role of Phospholipids in Mitochondrial Dynamics and Associated Diseases.

Front Biosci (Landmark Ed)

August 2025

University of Angers, MitoLab, Unité MITOVASC, UMR CNRS 6015, INSERM U1083, SFR ICAT, 49330 Angers, France.

The bioenergetic machinery of the cell is protected and structured within two layers of mitochondrial membranes. The mitochondrial inner membrane is extremely rich in proteins, including respiratory chain complexes, substrate transport proteins, ion exchangers, and structural fusion proteins. These proteins participate directly or indirectly in shaping the membrane's curvature and facilitating its folding, as well as promoting the formation of nanotubes, and proton-rich pockets known as cristae.

View Article and Find Full Text PDF

Introduction: Although peg-shaped lateral incisors are a common dental anomaly, the genetic mechanisms governing peg lateralis are poorly understood, particularly in cases where other associated anomalies are absent. Here, we aimed to identify potential candidate genes contributing to the development of non-syndromic peg lateralis via whole-exome sequencing (WES).

Methods: Saliva samples were collected from 20 unrelated Korean individuals with non-syndromic peg lateralis.

View Article and Find Full Text PDF

The state of the art in the thermodynamics of calix[4]resorcinarene derivatives and its metal ion complexes is briefly discussed in the introduction. This is followed by the synthesis and characterization of a recyclable calix[4]resorcinarene amide derivative (L). The 1H NMR analyses in CD3CN and CD3OD showed solvent-dependent conformational changes with a notable downfield chemical shift in the aromatic proton (H-2) in moving from deuterated methanol to acetonitrile, indicating an interaction of the solvent within the ligand cavity as suggested by molecular dynamic simulations.

View Article and Find Full Text PDF

Coelenterazine is the most common substrate for light-emitting reactions identified in luminous marine organisms. Among bioluminescent proteins engaging coelenterazine as a luciferin, Ca-regulated photoproteins form stable enzyme-substrate complexes offering thereby a unique opportunity to study their bioluminescence reactions in detail. Here, we used stopped-flow kinetics to investigate the formation of the emitters of recombinant aequorin, obelin, and W92F obelin activated with coelenterazine, as well as aequorin activated with coelenterazine-e.

View Article and Find Full Text PDF