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XB-ART-36123
Traffic. July 1, 2007; 8 (7): 893-903.

CVAK104 is a novel regulator of clathrin-mediated SNARE sorting.

Borner GH , Rana AA , Forster R , Harbour M , Smith JC , Robinson MS .


Abstract
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.

PubMed ID: 17587408
PMC ID: PMC2239300
Article link: Traffic.
Grant support: Wellcome Trust

Genes referenced: ap1m1 ap2m1 clint1 jun myc scyl2 tf tfap2a vti1a vti1b

Morpholinos referenced: ap1m1 MO1 ap2m1 MO1 scyl2 MO1

External Resources:
Article Images: [+] show captions

References:
Advani, 1999, Pubmed [+]


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