CVAK104 is a Novel Regulator of Clathrin‐mediated SNARE Sorting

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 demonst...

Full description

Saved in:
Bibliographic Details
Published in:Traffic (Copenhagen, Denmark) Denmark), 2007-07, Vol.8 (7), p.893-903
Main Authors: Borner, Georg H. H., Rana, Amer A., Forster, Rebecca, Harbour, Michael, Smith, James C., Robinson, Margaret S.
Format: Article
Language:English
Subjects:
Adaptor Proteins, Vesicular Transport - metabolism
Animals
AP‐1
AP‐2
Biological Transport
Cell Membrane - metabolism
Clathrin - metabolism
CVAK104
Endosomes - metabolism
epsinR
Evolution, Molecular
HeLa Cells
Humans
Mice
Original
Protein-Serine-Threonine Kinases - physiology
Qa-SNARE Proteins - metabolism
RNA, Small Interfering - metabolism
siRNA
SNARE
SNARE Proteins - metabolism
Xenopus
Xenopus - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1398-9219
1600-0854
DOI:10.1111/j.1600-0854.2007.00576.x