IndraLab

Statements

BAP1 activates cell adhesion. 11 / 11
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"As shown in XREF_FIG and quantified in XREF_FIG, Bap1 increased surface adhesion of wild-type V. cholerae, a Deltabap1DeltarbmC mutant, and a DeltavpsL mutant in monolayer minimal medium, while a control protein, bovine serum albumin (BSA), had no effect."
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"This suggests that communal Bap1 secreted by nearby biofilm cells may also increase surface adhesion of bystanders that have not yet been reprogrammed for biofilm matrix synthesis."
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"Exogenous Bap1 increases surface adhesion of planktonic bystanders as well."
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"The loss of function in the defective mutants is unlikely due to changes in the production or secretion level of the mutant protein (Supplementary Fig. 4a–d), and in all defective strains the adhesion defects can be rescued by WT Bap1/RbmC expressed from a plasmid (Supplementary Fig. 4e)."
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"Two of the proteins, RbmC and Bap1, are seemingly redundant paralogs that coat substrate surfaces and promotes cell adhesion, while another protein RbmA coats cell surfaces and promotes cell-cell cohesion."
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"Among the accessory proteins, RbmA has been shown to adhere biofilm-residing cells to each other , whereas Bap1 and RbmC contribute to cell-to-surface adhesion as well as to the formation of envelope structures surrounding Vc biofilm clusters ."
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"BAP1 loss reduced HAP1 cell adhesion/spreading (Fig. 1D) and proliferation (Fig. 1E), considered here to be readouts of cell fitness."
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"Bulk adhesion measurements for Bap1 and RbmC, which showed that Bap1 and RbmC contribute to surface adhesion in a surface-dependent manner, are largely consistent with our findings (31)."
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"Because exogenously provided Bap1 restored biofilm surface adhesion to a Deltabap1DeltarbmC mutant, we questioned whether Bap1 synthesis could be a joint venture in the biofilm community."
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"Bap1 mediates adhesion of bystander cells."
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"The functional difference between the two adhesins lies in the type of environment they interact with: RbmC was found to preferentially cause adhesion to biotic surfaces through its mucin-and N-glycan-binding domains, while Bap1 preferentially causes adhesion to abiotic surfaces and lipids through a loop within its β-propeller domain, and shows preferential expression near the biofilm-surface interface [64]."
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