During cell migration, actin assembly drives cell membrane protrusion, while microtubules (MTs) extend within protrusions to promote adhesion site turnover. Memo (mediator of ErbB2-driven cell motility) is an effector of the ErbB2 receptor tyrosine kinase involved in breast carcinoma cell migration. This effector may be important for mediating ErbB2-regulated changes in actin and MT dynamics during cell motility. Memo, a 297-amino-acid protein, has homology to class III nonheme iron-dependent dioxygenases, however it has not been shown to display metal binding or enzymatic activity. It has been shown to bind ErbB2 (Tyr-1227) phosphopeptide via its putative enzymatic active site. Memo and PLCγ1 interaction with ErbB2 is essential for HRG-induced chemotaxis. Furthermore, organization of the lamellipodial actin network is coordinated by signaling from Memo to the RhoA–mDia1 pathway localized to the plasma membrane. In addition, Memo may regulate actin dynamics by promoting cofilin depolymerizing and severing of F-actin.
Meira, M. et al. (2009) J. Cell Sci. 122:787.
Qiu, C. et al. (2008) J. Biol. Chem. 283:2734.
Zaoui, K. et al. (2008) J. Cell Biol. 183:401.
*For more information, see UniProt Accession Q9Y316
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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