HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine >
Japanese Journal of Veterinary Research >
Volume 57, Number 3 >

Structural implications of the EL(K/Q)(L/C)LD(A/G)DD sequence in the C-terminal cytoplasmic tail for proper targeting of anion exchanger 1 to the plasma membrane

Files in This Item:
JJVR57-3_1.pdf679.67 kBPDFView/Open
Please use this identifier to cite or link to this item:http://doi.org/10.14943/jjvr.57.3.135

Title: Structural implications of the EL(K/Q)(L/C)LD(A/G)DD sequence in the C-terminal cytoplasmic tail for proper targeting of anion exchanger 1 to the plasma membrane
Authors: Adachi, Hirokazu Browse this author
Ito, Daisuke Browse this author
Kurooka, Takao Browse this author
Otsuka, Yayoi Browse this author
Arashiki, Nobuto Browse this author
Sato, Kota Browse this author →KAKEN DB
Inaba, Mutsumi Browse this author →KAKEN DB
Keywords: AE1
band 3
carboxyl terminal tail
membrane trafficking
plasma membrane
Issue Date: Nov-2009
Publisher: Graduate School of Veterinary Medicine, Hokkaido University
Journal Title: Japanese Journal of Veterinary Research
Volume: 57
Issue: 3
Start Page: 135
End Page: 146
Abstract: While the C-terminal cytoplasmic tail of anion exchanger 1 (AE1, band 3) has been reported to possess important physiological roles, including one for proper membrane trafficking, its precise characteristics remain unclear. To clarify the overall structural consequences of the conserved sequence EL(K/Q)(L/C)LD(A/G)DD, containing the core binding sequence LDADD for carbonic anhydrase II, in the C-terminal region, we analyzed the membrane expression and turnover of bovine AE1 with a series of truncation and substitution mutations in HEK293 cells. Immunofluorescence microscopy and cell-surface biotinylation demonstrated that truncation mutants missing 18 C-terminal residues targeted the plasma membrane, but the one lacking the conserved region, by truncation of 28 amino acid residues, was retained inside the cells. Substitutions of Ala for Glu901, Leu902, Leu905, and Asp906 in the sequence E901L(K/Q)(L/C)LDADD909 of bovine AE1 or those in the corresponding murine sequence also caused intracellular retention, though these mutants had half-lives comparable to that for wild-type AE1. These data demonstrate that the conserved amino acid residues Glu1, Leu2, Leu5, and Asp6 in the EL(K/Q)(L/C)LD(A/G)DD region have essential structural consequences in stable expression of AE1 at the plasma membrane regardless of the ability in binding to carbonic anhydrase II of this region.
Type: bulletin (article)
URI: http://hdl.handle.net/2115/39935
Appears in Collections:Japanese Journal of Veterinary Research > Volume 57, Number 3

Submitter: 獣医学部図書室

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University