RGD Reference Report - Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels. - Rat Genome Database

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Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels.

Authors: Takimoto, K  Yang, EK  Conforti, L 
Citation: Takimoto K, etal., J Biol Chem 2002 Jul 26;277(30):26904-11.
RGD ID: 625553
Pubmed: PMID:12006572   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M203651200   (Journal Full-text)

The Ca(2+)-binding proteins KChIP1-4 (KChIP3 is also known as DREAM and calsenilin) act as auxiliary subunits for voltage-gated K(+) channels in the Kv4 family. Here we identify three splicing isoforms of rat KChIP2 with variable N-terminal peptides. The two longer isoforms, which contain the 32-amino acid peptide, produce larger increases in Kv4.3 protein level and current density and more effectively localize themselves and their associated channels at the plasma membrane than the shortest variant. The 32-amino acid peptide contains potential palmitoylation cysteines. Metabolic labeling demonstrates that these cysteines in the KChIP2 isoforms, as well as the corresponding sites in KChIP3, are palmitoylated. Mutating these cysteines reduces their plasma membrane localization and the enhancement of Kv4.3 current density. Thus, palmitoylation of the KChIP auxiliary subunits controls plasma membrane localization of their associated channels.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Kcnip2  (potassium voltage-gated channel interacting protein 2)
Kcnip2_v1  (potassium voltage-gated channel interacting protein 2, variant 1)
Kcnip2_v2  (potassium voltage-gated channel interacting protein 2, variant 2)
Kcnip2_v3  (potassium voltage-gated channel interacting protein 2, variant 3)


Additional Information