[HTML][HTML] Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
Thrombospondin induces reorganization of the actin cytoskeleton and restructuring of focal
adhesions. This activity is localized to amino acids 17–35 in the N-terminal heparin-binding
domain of thrombospondin and can be replicated by a peptide (hep I) with this sequence.
Thrombospondin/hep I stimulate focal adhesion disassembly through a mechanism
involving phosphoinositide 3-kinase activation. However, the receptor for this
thrombospondin sequence is unknown. We now report that calreticulin on the cell surface …
adhesions. This activity is localized to amino acids 17–35 in the N-terminal heparin-binding
domain of thrombospondin and can be replicated by a peptide (hep I) with this sequence.
Thrombospondin/hep I stimulate focal adhesion disassembly through a mechanism
involving phosphoinositide 3-kinase activation. However, the receptor for this
thrombospondin sequence is unknown. We now report that calreticulin on the cell surface …
