Fig 1: Whole cell patch clamp recording of WT and TRPM5 N932Q mutant transiently transfected in HEK293 cells. (A) Individual currents recorded using a ramp protocol depicted in the inset. (B) Current vs. voltage relationship shows a decreased current in TRPM5 N932Q mutant without major alterations of the biophysical properties. Statistical test using two-tailed Student T-test *P < 0.05, **P < 0.01.
Fig 2: N-glycosylation site of TRPM4 and TRPM5. (A) A bioinformatic search reveals a putative site for N-linked glycosylation in TRPM4 that is conserved in different organisms and the closely related TRPM5. (B) Illustration showing the location of N-linked glycosylation site in the pore-forming region between transmembrane segments 5 and 6 of TRPM4 and TRPM5.
Fig 3: Deglycosylation and biotinylation of TRPM5. (A) Treatment with PNGase F demonstrates that unglycosylated WT TRPM5 has a similar molecular weight to the TRPM5 N932Q mutant. (B) Cell surface biotinylation of HEK293 cells transiently transfected with WT or TRPM5 N932Q mutant constructs shows expression of both WT and mutant at the total level and at the cell surface. (C) Treatment with Endo H removes some of the glycosylation in both input and biotinylated fractions.
Supplier Page from Abcam for Anti-TRPM5 antibody [EPR7504]