ArticleProtein science : a publication of the Protein Society2006
pH driven conformational dynamics and dimer-to-monomer transition in DLC8.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- mTOR Senses Intracellular pH through Lysosome Dispersion from RHEB.BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Plant glutathione biosynthesis revisited: redox-mediated activation of glutamylcysteine ligase does not require homo-dimerization.The Biochemical journal · 2019Article
- Loss of sirtuin 1 and mitofusin 2 contributes to enhanced ischemia/reperfusion injury in aged livers.Aging cell · 2018Article
- Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.The Journal of biological chemistry · 2013Article
- Dynein light chain 1 (LC8) association enhances microtubule stability and promotes microtubule bundling.The Journal of biological chemistry · 2012Article
- SPARC stimulates neuronal differentiation of medulloblastoma cells via the Notch1/STAT3 pathway.Cancer research · 2011Article
- DYNLL/LC8 protein controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9.The Journal of biological chemistry · 2011Article
- Resonance Assignments and Secondary Structure Analysis of Dynein Light Chain 8 by Magic Angle Spinning NMR Spectroscopy.Canadian journal of chemistry · 2011Article
- Cathepsin B facilitates autophagy-mediated apoptosis in SPARC overexpressed primitive neuroectodermal tumor cells.Cell death and differentiation · 2010Article
- Structure-function-folding relationships and native energy landscape of dynein light chain protein: nuclear magnetic resonance insights.Journal of biosciences · 2009Review
- NMR investigations on residue level unfolding thermodynamics in DLC8 dimer by temperature dependent native state hydrogen exchange.Journal of biomolecular NMR · 2009Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Dynein light chain protein, a part of the cytoplasmic motor assembly, is a homodimer at physiological pH and dissociates below pH 4.5 to a monomer. The dimer binds to a variety of cargo, whereas the monomer does not bind any of the target proteins. We report here the pH induced stepwise structural and motional changes in the protein, as derived from line broadening and 15N transverse relaxation measurements. At pH 7 and below until 5, partial protonation and consequent interconversion between molecules carrying protonated and neutral histidines, causes conformational dynamics in the dimeric protein and this increases with decreasing pH. Enhanced dynamics in turn leads to partial loosening of the structure. This would have implications for different efficacies of binding by target proteins due to small variations in pH in different parts of the cell, and hence for cargo trafficking from one part to another. Below pH 5, enhanced charge repulsions, partial loss of hydrophobic interactions, and destabilization of H-bonds across the dimer interface cause further loosening of the dimeric structure, leading eventually to the dissociation of the dimer.
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