Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 11, Pages 9246-9256Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.130427
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Funding
- United Kingdom Biotechnology and Biological Science Research Council
- Wellcome Trust [077503, 079819, 085464, 068779]
- SRCD
- European Union [RII3-CT-2004-506008]
- BBSRC [BB/G530417/1] Funding Source: UKRI
- MRC [G0800038] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G530417/1] Funding Source: researchfish
- Medical Research Council [G0800038] Funding Source: researchfish
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The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stage-regulated expression in the non-replicative vector-transmitted stages of the kinetoplastid parasite, Leishmania major, the causative agent of human cutaneous leishmaniasis. Previous studies have demonstrated that SHERP localizes as a peripheral membrane protein on the cytosolic face of the endoplasmic reticulum and on outer mitochondrial membranes, whereas its high copy number suggests a critical function in vivo. However, the absence of defined domains or identifiable orthologues, together with lack of a clear phenotype in transgenic parasites lacking SHERP, has limited functional understanding of this protein. Here, we use a combination of biophysical and biochemical methods to demonstrate that SHERP can be induced to adopt a globular fold in the presence of anionic lipids or SDS. Cross-linking and binding studies suggest that SHERP has the potential to form a complex with the vacuolar type H+-ATPase. Taken together, these results suggest that SHERP may function in modulating cellular processes related to membrane organization and/or acidification during vector transmission of infective Leishmania.
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