Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1858, Issue 11, Pages 2763-2768Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2016.06.026
Keywords
Membrane; Lipid; Lipidation; Membrane protein; Aquaporin; Posttranslational modification
Categories
Funding
- Ministry of Higher Education and Scientific Research of the Kurdistan Regional Government [1391]
- Fight for Sight UK [1584/1585]
- Leverhulme Trust [RPG-2012-554]
- Fight for Sight [1584/85] Funding Source: researchfish
Ask authors/readers for more resources
The lens fiber major intrinsic protein (otherwise known as aquaporin-0 (AQP0), MIP26 and MP26) has been examined by mass spectrometry (MS) in order to determine the speciation of acyl modifications to the side chains of lysine residues and the N-terminal amino group. The speciation of acyl modifications to the side chain of one specific, highly conserved lysine residue (1(238) and the N-terminal amino group of human and bovine AQPO revealed, in decreasing order of abundance, oleoyl, palmitoyl, stearoyl, eicosenoyl, dihomo-gamma-linolenoyl, palmitoleoyl and eicosadienoyl modifications. In the case of human AQPO, an arachidonoyl modification was also found at the N-terminus. The relative abundances of these modifications mirror the fatty acid composition of lens phosphatidylethanolamine lipids. This lipid class would be expected to be concentrated in the inner leaflet of the lens fiber membrane to which each of the potential AQPO lipidation sites is proximal. Our data evidence a broad lipidation profile that is both species and site independent, suggesting a chemical-based ester aminolysis mechanism to explain such modifications. (C) 2016 Published by Elsevier B.V.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available