Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor
Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor
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DOI:
10.1016/j.jmb.2006.06.011
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发表时间:
2006-07-28
影响因子:
5.6
通讯作者:
Hartmann-Petersen, Rasmus
中科院分区:
文献类型:
--
作者:
Jorgensen, Jakob Ploug;Lauridsen, Anne-Marie;Hartmann-Petersen, Rasmus
We have identified Adrm1 as a novel component of the regulatory ATPase complex of the 26 S proteasome: Adrml was precipitated with an antibody to proteasomes and vice versa. Adrm1 co-migrated with proteasomes on gel-filtration chromatography and non-denaturing polyacrylamide gel electrophoresis. Adrml has been described as an interferon-gamma-inducible, heavily glycosylated membrane protein of 110 kDa. However, we found Adrm1 in mouse tissues only as a 42 kDa peptide, corresponding to the mass of the non-glycosylated peptide chain, and it could not be induced in HeLa cells with interferon. Adrml was present almost exclusively in soluble 26 S proteasomes, albeit a small fraction was membrane-associated, like proteasomes. Adrml was found in cells in amounts equimolar with S6a, a 26 S proteasome subunit. HeLa cells contain no pool of free Adrml but recombinant Adrml could bind to pre-existing 26 S proteasomes in cell extracts. Adrml may be distantly related to the yeast proteasome subunit Rpn13, mutants of which are reported to display no obvious phenotype. Accordingly, knock-down of Adrml in HeLa cells had no effect on the amount of proteasomes, or on degradation of bulk cell protein, or accumulation of polyubiquitinylated proteins. This indicates that Adrm1 has a specialised role in proteasome function. (c) 2006 Elsevier Ltd. All rights reserved.