IndraLab

Statements


CDK5 phosphorylates CACNA1B. 7 / 7
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rlimsp
"The increased association between Cdk5-phosphorylated CRMP2 and CaV2.2 was reduced by (S)-LCM in vitro and in vivo."

sparser
"To determine whether CaV2.2 channel phosphorylation by Cdk5 favors neurotransmitter release, primary neurons were transduced with a bicistronic herpes simplex virus (HSV) expressing wildtype CaV2.2 and the miniature excitatory postsynaptic currents (mEPSC) were recorded."

reach
"We previously characterized (S)-lacosamide ((S)-LCM) as a small molecule inhibiting both CRMP2 phosphorylation by Cdk5 and CaV2.2 activity in sensory neurons."

sparser
"With the exception of lacosamide, which reduced the association between Cdk5-phosphorylated CRMP2 and CaV2.2 in vitro and in vivo ( xref ), the binding of small molecules to CRMP2 has rarely been reported."

sparser
"The increased association between Cdk5-phosphorylated CRMP2 and CaV2.2 was reduced by (S)-LCM in vitro and in vivo."

sparser
"In an alternative approach, a dominant-negative CDK5 construct was used to show that CDK5 phosphorylates a conserved serine residue in the C-terminal domain of Cav2.2."

sparser
"Hence, unlike P/Q-type (CaV2.1) Ca 2+ channels, phosphorylation of CaV2.2 by Cdk5 favors neurotransmitters release."