.png){kind=icon}
.png){kind=icon}
Return
Two-Step Membrane Binding of NDPK-B Induces Membrane Fluidity Decrease and Changes in Lipid Lateral Organization and Protein Cluster Formation
.png){kind=icon}
PRE
AI
DOI：10.1021/acs.langmuir.6b03789.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
Nucleoside diphosphate kinases (NDPKs) are crucial elements in a wide array of cellular physiological or pathophysiological processes such as apoptosis, proliferation, or metastasis formation. Among the NDPK isoenzymes, NDPK-B, a cytoplasmic protein, was reported to be associated with several biological membranes such as plasma or endoplasmic reticulum membranes. Using several membrane models (liposomes, lipid monolayers, and supported lipid bilayers) associated with biophysical approaches, we show that lipid membrane binding occurs in a two-step process: first, initiation by a strong electrostatic adsorption process and followed by shallow penetration of the protein within the membrane. The NDPK-B binding leads to a decrease in membrane fluidity and formation of protein patches. The ability of NDPK-B to form microdomains at the membrane level may be related to protein-protein interactions triggered by its association with anionic phospholipids. Such accumulation of NDPK-B would amplify its effects in functional platform formation and protein recruitment at the membrane.
Keywords:
DIPHOSPHATE-KINASE-B
ANTIMICROBIAL PEPTIDES
LAURDAN FLUORESCENCE
CELL-ADHESION
HISTIDINE PHOSPHORYLATION
SUBCELLULAR-LOCALIZATION
PHOSPHOLIPID MONOLAYERS
SUPPRESSOR NM23-H2
METASTASIS
MECHANISM
AI Summary
Key information extracted from the uploaded paper, including a brief overview, abstract, background, key highlights, visual analysis, and future outlook.
Journal
IF:
3.9
Papers:
5.4W
Citations:
10.6W
View more organizations