CVAK104 is a novel regulator of clathrin-mediated SNARE sorting

Georg H. H. Borner, Amer A. Rana, Rebecca Forster, Michael Harbour, James C. Smith, Margaret S. Robinson

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)


Clathrin-coated vesicles (CCVs) mediate transport between the plasma membrane, endosomes and the trans Golgi network. Using comparative proteomics, we have identified coated-vesicle-associated kinase of 104 kDa (CVAK104) as a candidate accessory protein for CCV-mediated trafficking. Here, we demonstrate that the protein colocalizes with clathrin and adaptor protein-1 (AP-1), and that it is associated with a transferrin-positive endosomal compartment. Consistent with these observations, clathrin as well as the cargo adaptors AP-1 and epsinR can be coimmunoprecipitated with CVAK104. Small interfering RNA (siRNA) knockdown of CVAK104 in HeLa cells results in selective loss of the SNARE proteins syntaxin 8 and vti1b from CCVs. Morpholino-mediated knockdown of CVAK104 in Xenopus tropicalis causes severe developmental defects, including a bent body axis and ventral oedema. Thus, CVAK104 is an evolutionarily conserved protein involved in SNARE sorting that is essential for normal embryonic development.

Original languageEnglish
Pages (from-to)893-903
Number of pages11
Issue number7
Publication statusPublished - Jul 2007


  • AP-1
  • AP-2
  • CVAK104
  • epsinR
  • siRNA
  • Xenopus

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