%0 Journal Article
%T Vigilin interacts with signal peptide peptidase
%A Stephen HJ Lu
%A Amy HW Jeon
%A Gerold Schmitt-Ulms
%A Seema Qamar
%A Roger Dodd
%A Beth McDonald
%A Yi Li
%A William Meadows
%A Katie Cox
%A Christopher Bohm
%A Fusheng Chen
%A Paul Fraser
%A Peter St George-Hyslop
%J Proteome Science
%D 2012
%I BioMed Central
%R 10.1186/1477-5956-10-33
%X In this study, an unbiased iTRAQ-labeling mass spectrometry approach was used to identify SPP-interacting proteins. We found that vigilin, a ubiquitous multi-KH domain containing cytoplasmic protein involved in RNA binding and protein translation control, selectively enriched with SPP. Vigilin interacted with SPP and both proteins co-localized in restricted intracellular domains near the ER, biochemically co-fractionated and were part of the same 450 kDa complex on BN gels. However, vigilin does not alter the protease activity of SPP, suggesting that the SPP-vigilin interaction might be involved in the non-proteolytic functions of SPP.We have identified and validated vigilin as a novel interacting partner of SPP that could play an important role in the non-proteolytic functions of SPP. This data adds further weight to the idea that intramembrane-cleaving aspartyl proteases, such as presenilin and SPPs, could have other functions besides the proteolysis of short membrane stubs.
%K Signal peptide peptidase
%K Vigilin
%K Biochemistry
%K Intramembrane-cleaving aspartyl protease
%K Non-proteolytic function
%K Interactome
%U http://www.proteomesci.com/content/10/1/33/abstract