Msba Flippase
Msba Flippase - Related Videos
09:45
Mapping and Application of Enhancer-trap Flippase Expression in Larval and Adult Drosophila CNS
0 Views •
Cited by 7 •
2011
We describe a Flippase-induced intersectional Gal80/Gal4 repression (FINGR) method, allowing tissue-specific FLP to determine Gal80 expression patterns. Wherever Gal4 and FLP overlap, Gal4 expression is turned on (Gal80 flipped out) or off (Gal80 flipped in). The FINGR method is versatile for clonal analysis and neural circuit mapping.
11:36
Rapid and Efficient Generation of Recombinant Human Pluripotent Stem Cells by Recombinase-mediated Cassette Exchange in the AAVS1 Locus
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Cited by 3 •
2016
Here we report a rapid and efficient gene editing method based on RMCE in the AAVS1 locus of human Pluripotent Stem Cells (hPSCs) that improves upon previously described systems. Using this technique, isogenic lines can be rapidly and reliably generated for proper comparative studies, facilitating transgenesis-mediated research with hPSCs.
06:30
Cell Lineage Analyses and Gene Function Studies Using Twin-spot MARCM
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Cited by 2 •
2017
Here, we present a protocol for a mosaic labeling technique that permits the visualization of neurons derived from a common progenitor cell in two distinct colors. This facilitates neural lineage analysis with the capability of birth-dating individual neurons and studying gene function in the same neurons of different individuals.
FAQs
MsbA couples ATP binding and hydrolysis at its cytoplasmic nucleotide-binding domains to conformational changes in its transmembrane domains. These linked movements alter the orientation of the membrane-spanning region, allowing the transporter to present a substrate-binding pathway toward different sides of the bacterial inner membrane. This coupling converts chemical energy into directional lipid movement.
The transmembrane domains do more than provide a passage through the membrane. Their alternating conformations help MsbA recognize compatible phospholipids and lipid A precursors, then expose the binding pathway to opposite sides of the membrane. Because the nucleotide-binding domains control these conformational transitions, substrate handling and directionality remain coordinated rather than occurring as unrestricted diffusion.
MsbA must distinguish particular phospholipids and lipid A precursors from the broader collection of molecules present in the membrane. That selectivity connects transport to membrane composition and cell-envelope assembly. Studying which substrates are handled by the transporter therefore helps explain how bacterial cells organize envelope components while avoiding indiscriminate movement of membrane material.
Structural studies can show how the nucleotide-binding domains and transmembrane domains are arranged and how their relative conformations change during transport. They also help investigators examine the substrate-binding pathway and its exposure to opposite membrane sides. These observations provide a molecular framework for understanding how an ABC transporter recognizes lipids and produces directional movement.
MsbA contributes to the export of components needed for the bacterial cell envelope, including lipid A precursors. Because this activity supports envelope-related physiology, the transporter is relevant to antimicrobial research. Examining its transport mechanism may also identify structural or functional features that can be considered when investigating ways to interfere with bacterial membrane and envelope maintenance.
By moving selected phospholipids and lipid A precursors across the inner membrane, MsbA links molecular transport to larger cellular processes. Its activity helps maintain membrane composition and supports cell-envelope assembly, so changes in transporter performance can be interpreted in the context of bacterial envelope organization. This makes MsbA useful for studying membrane biology as well as transporter mechanism.