A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KChIP1 and Kv4 potassium channels

Flowerdew, SE and Burgoyne, RD ORCID: 0000-0002-9219-0387 (2009) A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KChIP1 and Kv4 potassium channels Biochemical Journal, 418 (3). pp. 529-540. ISSN 0264-6021, 1470-8728

Text revised Flowerdew and Burgoyne with figures .pdf - Unspecified Download (1MB)

Abstract

The KChIPs (K⁺ channel-interacting proteins) are EF hand-containing proteins required for the traffic of channel-forming Kv4 K⁺ subunits to the plasma membrane. KChIP1 is targeted, through N-terminal myristoylation, to intracellular vesicles that appear to be trafficking intermediates from the ER (endoplasmic reticulum) to the Golgi but differ from those underlying conventional ER-Golgi traffic. To define KChIP1 vesicles and the traffic pathway followed by Kv4/KChIP1 traffic, we examined their relationship to potential SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) proteins mediating the trafficking step. To distinguish Kv4/ KChIP1 from conventional constitutive traffic, we compared it to the traffic of the VSVG (vesicular-stomatitis virus G-protein). Expression of KChIP with single or triple EF hand mutations quantitatively inhibited Kv4/KChIP1 traffic to the cell surface but had no effect on VSVG traffic. KChIP1-expressing vesicles co-localized with the SNARE proteins Vti1a and VAMP7 (vesicle-associated membrane protein 7), but not with the components of two other ER-Golgi SNARE complexes. siRNA (small interfering RNA)-mediated knockdown of Vti1a or VAMP7 inhibited Kv4/KChIP1 traffic to the plasma membrane in HeLa and Neuro2A cells. Vti1a and VAMP7 siRNA had no effect on VSVG traffic or that of Kv4.2 when stimulated by KChIP2, a KChIP with different intrinsic membrane targeting compared with KChIP1. The present results suggest that a SNARE complex containing VAMP7 and Vti1a defines a novel traffic pathway to the cell surface in both neuronal and non-neuronal cells.

Item Type:	Article
Additional Information:	Journal article The Biochemical journal Biochem J. 2009 Jan 13. ## TULIP Type: Articles/Papers (Journal) ##
Uncontrolled Keywords:	calcium-binding protein, K+ channel-interacting protein (KChIP), potassium channel, neuronal calcium sensor (NCS) protein, soluble N-ethylmaleimide-sensitive fusion proteinattachment protein receptor (SNARE)
Depositing User:	Symplectic Admin
Date Deposited:	05 Nov 2014 15:29
Last Modified:	24 Jan 2026 00:22
DOI:	10.1042/BJ20081736
Related Websites:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/2001479
Disclaimer:	The University of Liverpool is not responsible for content contained on other websites from links within repository metadata. Please contact us if you notice anything that appears incorrect or inappropriate.