17 research outputs found
Ca2+ Signaling and Cytoskeleton Reorganization in Endothelial Cells Stimulated by Bradykinin
No full textInvolvement of CD44 and its variant isoforms in membrane-cytoskeleton interaction, cell adhesion and tumor metastasis
No full textDisruption of intracerebral progression of rat C6 glioblastoma by in vivo treatment with anti-CD44 monoclonal antibody
No full textA novel PKC-regulated mechanism controls CD44-ezrin association and directional cell motility
No full textA novel PKC-regulated mechanism controls CD44-ezrin association and directional cell motility. The dynamic assembly and disassembly of membrane-cytoskeleton junctional complexes is critical in cell migration. Here we describe a novel phosphorylation mechanism that regulates the hyaluronan receptor CD44. In resting cells, CD44 is constitutively phosphorylated at a single serine residue, Ser325. After protein kinase C is activated, a switch in phosphorylation results in CD44 being phosphorylated solely at an alternative residue, Ser291. Using fluorescence resonance energy transfer (FRET) monitored by fluorescence lifetime imaging microscopy (FLIM) and chemotaxis assays we show that phosphorylation of Ser291 modulates the interaction between CD44 and the cytoskeletal linker protein ezrin in vivo, and that this phosphorylation is critical for CD44-dependent directional cell motility
Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali
No full textLocalization of CD44, the hyaluronate receptor; on the plasma membrane of osteocytes and osteoclasts in rat tibiae
No full textMolecular mechanisms regulating the hyaluronan binding activity of the adhesion protein CD44
No full textA novel PKC-regulated mechanism controls CD44–ezrin association and directional cell motility
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