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Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates Kv1 channel axonal targeting.

Authors: Vacher, H  Yang, JW  Cerda, O  Autillo-Touati, A  Dargent, B  Trimmer, JS 
Citation: Vacher H, etal., J Cell Biol. 2011 Mar 7;192(5):813-24. doi: 10.1083/jcb.201007113. Epub 2011 Feb 28.
Pubmed: (View Article at PubMed) PMID:21357749
DOI: Full-text: DOI:10.1083/jcb.201007113

Kv1 channels are concentrated at specific sites in the axonal membrane, where they regulate neuronal excitability. Establishing these distributions requires regulated dissociation of Kv1 channels from the neuronal trafficking machinery and their subsequent insertion into the axonal membrane. We find that the auxiliary Kvbeta2 subunit of Kv1 channels purified from brain is phosphorylated on serine residues 9 and 31, and that cyclin-dependent kinase (Cdk)-mediated phosphorylation at these sites negatively regulates the interaction of Kvbeta2 with the microtubule plus end-tracking protein EB1. Endogenous Cdks, EB1, and Kvbeta2 phosphorylated at serine 31 are colocalized in the axons of cultured hippocampal neurons, with enrichment at the axon initial segment (AIS). Acute inhibition of Cdk activity leads to intracellular accumulation of EB1, Kvbeta2, and Kv1 channel subunits within the AIS. These studies reveal a new regulatory mechanism for the targeting of Kv1 complexes to the axonal membrane through the reversible Cdk phosphorylation-dependent binding of Kvbeta2 to EB1.


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RGD Object Information
RGD ID: 10047144
Created: 2015-07-11
Species: All species
Last Modified: 2015-07-11
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.