CVAK104 is a novel regulator of clathrin-mediated SNARE sorting

Borner, Georg H. H., Rana, Amer A. ORCID: https://orcid.org/0000-0002-2330-4643, Forster, Rebecca, Harbour, Michael, Smith, James C. and Robinson, Margaret S. (2007) CVAK104 is a novel regulator of clathrin-mediated SNARE sorting. Traffic, 8 (7). pp. 893-903. ISSN 1398-9219

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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.

Item Type:	Article
Uncontrolled Keywords:	ap-1,ap-2,cvak104,epsinr,sirna,snare,xenopus,structural biology,biochemistry,molecular biology,genetics,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:	Faculty of Science > School of Biological Sciences
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	01 Nov 2022 14:32
Last Modified:	02 Nov 2022 13:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/89475
DOI:	10.1111/j.1600-0854.2007.00576.x

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