ArticleCytoskeleton (Hoboken, N.J.)2010
Localization of MglA, an essential gliding motility protein in Myxococcus xanthus.
Article in Cytoskeleton (Hoboken, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Structural and biophysical insights into RomR, MglB, and MglC interactions involved in regulating cell polarity in Myxococcus xanthus.The Journal of biological chemistry · 2025Article
- Mathematical modeling of mechanosensitive reversal control inFrontiers in microbiology · 2023Article
- Spatial control of the GTPase MglA by localized RomR-RomX GEF and MglB GAP activities enables Myxococcus xanthus motility.Nature microbiology · 2019Article
- MglC, a Paralog of Myxococcus xanthus GTPase-Activating Protein MglB, Plays a Divergent Role in Motility Regulation.Journal of bacteriology · 2016Article
- The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions.The Journal of cell biology · 2015Article
- An evolutionary link between capsular biogenesis and surface motility in bacteria.Nature reviews. Microbiology · 2015Review
- Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity.The EMBO journal · 2011Article
- Global analysis of phase variation in Myxococcus xanthus.Molecular microbiology · 2011Article
- Poles apart: prokaryotic polar organelles and their spatial regulation.Cold Spring Harbor perspectives in biology · 2011Review
- Uncovering the mystery of gliding motility in the myxobacteria.Annual review of genetics · 2011Review
- Effects of site-directed mutagenesis of mglA on motility and swarming of Myxococcus xanthus.BMC microbiology · 2010Article
- Cell polarity/motility in bacteria: closer to eukaryotes than expected?The EMBO journal · 2010Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
MglA, a 22-kDa protein related to monomeric GTPases, is required for the normal operation of the A (Adventurous) and S (Social) motility and for multicellular development of Myxococcus xanthus. To determine how MglA controls A- and S-motility, MglA was assayed biochemically and its cellular location was determined. His-tagged MglA hydrolyzed GTP slowly in vitro at a rate nearly identical to that of Ras showing that MglA has GTPase activity. Immunofluorescence microscopy of fixed cells from liquid showed that MglA was associated with helical track similar to the MreB spiral that spanned the length of the cell. The distribution pattern of MglA depended on the type of surface from which cells were harvested. In cells gliding on 1.5% (w/v) agar, the helical pattern gave way to punctate clusters of MglA-Yfp at the poles and along the long axis (lateral clusters). The lateral clusters emerged near the leading pole as the cell advanced coincident with a decrease in the intensity of the MglA-Yfp cluster at the leading pole. Newly formed lateral clusters remained fixed with regard to the substratum as the cell moved forward, similar to focal adhesion complexes described for AglZ, a protein partner of MglA. Lateral clusters did not form in cells gliding in methylcellulose, a polymer that stimulates S-motility at low cell density; rather MglA-Yfp was diffuse in the cytoplasm and more concentrated at the poles. The results suggest that conditions that favor S-motility prevent the formation of lateral clusters of MglA, which are associated with A-motility functions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.