v5.1.0.3
Cicer data from the Legume Information System
Type | Domain |
Description | Phosphoinositide-specific phospholipase C (PI-PLC), also known as 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase, plays a role in the inositol phospholipid signaling by hydrolysing phosphatidylinositol-4,5-bisphosphate to produce the second messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). These cause the increase of intracellular calcium concentration and the activation of protein kinase C (PKC), respectively.The PLC family in murine or human species is comprised of multiple subtypes. On the basis of their structure, they have been divided into five classes, beta (beta-1, 2, 3 and 4), gamma (gamma-1 and 2), delta (delta-1, 3 and 4), epsilon, zeta, and eta types [ , ].PLC-beta-1 is the predominant PLC isoform in the brain. PLC-beta-1 knockout mice exhibit behavioral abnormalities as a result of disrupted cortical development and plasticity [ ]. PLC-beta-1 is involved in cell cycle control [, ] and in development and fertility [, ]. It has an important role in the control of mouse oocyte meiosis. PLC beta 1 is first exclusively localised to the nucleus and then migrates to the cytoplasm when the oocyte is fully grown; this chronology being crucial for the production of competent oocytes []. It regulates neuronal activity in the cerebral cortex and hippocampus, and has been implicated for participations in diverse critical functions related to forebrain diseases such as schizophrenia and epileptic encephalopathy [, ].PLC-beta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs (represented by this entry), a PLC catalytic core, and a single C2 domain. |
Short Name | PLC-beta1_EF |