TY - JOUR AU - Wong, Raymond AU - Fabian, Lacramioara AU - Forer, Arthur AU - Brill, Julie A. PY - 2007 DA - 2007/05/17 TI - Phospholipase C and myosin light chain kinase inhibition define a common step in actin regulation during cytokinesis JO - BMC Cell Biology SP - 15 VL - 8 IS - 1 AB - Phosphatidylinositol 4,5-bisphosphate (PIP2) is required for successful completion of cytokinesis. In addition, both PIP2 and phosphoinositide-specific phospholipase C (PLC) have been localized to the cleavage furrow of dividing mammalian cells. PLC hydrolyzes PIP2 to yield diacylglycerol (DAG) and inositol trisphosphate (IP3), which in turn induces calcium (Ca2+) release from the ER. Several studies suggest PIP2 must be hydrolyzed continuously for continued cleavage furrow ingression. The majority of these studies employ the N-substituted maleimide U73122 as an inhibitor of PLC. However, the specificity of U73122 is unclear, as its active group closely resembles the non-specific alkylating agent N-ethylmaleimide (NEM). In addition, the pathway by which PIP2 regulates cytokinesis remains to be elucidated. SN - 1471-2121 UR - https://doi.org/10.1186/1471-2121-8-15 DO - 10.1186/1471-2121-8-15 ID - Wong2007 ER -