Description: Alternative splicing removes the PDZ-binding motif of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1), abrogating binding to Partitioning defective 3 homolog (PARD3). The G protein-activated PLCB1 can directly interact with cell polarity proteins Partitioning defective 3 homolog (PARD3) and Partitioning defective 6 homolog alpha (PARD6A) to form protein complexes in the cell, which potentially modulate G protein-activated PLCB1 activity in cell polarity formation and asymmetric cell division.
Participants: (1) 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1) (2) Partitioning defective 3 homolog (PARD3)
(1) G-protein-activated phospholipase C-beta, new partners for cell polarity proteins Par3 and Par6.Cai et al. Oncogene (2005) (2) The extreme C-terminal region of phospholipase Cbeta1 determines subcellular localization and function; the "b" splice variant mediates alpha1-adrenergic receptor responses in cardiomyocytes.Grubb et al. FASEB J. (2008)
