Fig. 5: TPM4 mediates actin reorganization coupled with regulation of glycolysis.
From: TPM4 condensates glycolytic enzymes and facilitates actin reorganization under hyperosmotic stress
a Left: representative images of PFKM (green) and phalloidin (magenta) immunofluorescence staining in MDA-MB-231 wild-type cells treated with 100 mM sorbitol for 3 min. Scale bar, 20 μm. Right: line scan plot showing the intensity distribution of PFKM and actin filaments along the yellow line. b Representative images of PFKM (green) and phalloidin (magenta) immunofluorescence staining in MDA-MB-231 TPM4 KO cells treated with 100 mM sorbitol for 3 min. Scale bar, 20 μm. Right: line scan plot showing the intensity distribution of PFKM and actin filaments along the yellow line. c Representative images of phalloidin (magenta) immunofluorescence staining in wild-type and TPM4 KO cells treated with 100 mM sorbitol for 1 h. Scale bars, 20 μm. d Representative images of TPM4 (green) and PFKM (magenta) immunofluorescence staining in mouse kidney tissue sections. Scale bar, 20 μm. e A model (created with BioRender.com) for TPM4 phase separation-mediated reorganization of multiple glycolytic enzymes. Upon hyperosmotic stress, TPM4 undergoes phase separation, recruiting 10 essential glycolytic enzymes to upregulate glycolysis and support energy for actin reorganization.
