Universidad Peruana Cayetano Heredia

Structural basis of molecular recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at membrane surfaces

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dc.contributor.author Moore, B.
dc.contributor.author Miles, A.J.
dc.contributor.author Guerra-Giraldez, C.
dc.contributor.author Simpson, P.
dc.contributor.author Iwata, M.
dc.contributor.author Wallace, B.A.
dc.contributor.author Matthews, S.J.
dc.contributor.author Smith, D.F.
dc.contributor.author Brown, K.A.
dc.date.accessioned 2022-01-18T19:26:50Z
dc.date.available 2022-01-18T19:26:50Z
dc.date.issued 2011
dc.identifier.uri https://hdl.handle.net/20.500.12866/10927
dc.description.abstract The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stageregulated 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. en_US
dc.language.iso eng
dc.publisher Elsevier
dc.relation.ispartofseries Journal of Biological Chemistry
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject Controlled Study en_US
dc.subject Unclassified Drug en_US
dc.subject Protein Binding en_US
dc.subject Protozoan Proteins en_US
dc.subject Leishmania en_US
dc.subject Bacterial Strain en_US
dc.subject In-Vivo en_US
dc.subject Protein Analysis en_US
dc.subject Plants (Botany) en_US
dc.subject Protein Function en_US
dc.subject Protein Localization en_US
dc.subject Protein Structure en_US
dc.subject Biochemistry en_US
dc.subject Biological Membranes en_US
dc.subject Causative Agents en_US
dc.subject Cell Membranes en_US
dc.subject Cellular Process en_US
dc.subject Complex Formation en_US
dc.subject Copy Number en_US
dc.subject Critical Functions en_US
dc.subject Cytosolic en_US
dc.subject Endoplasmic Reticulum en_US
dc.subject Kinetoplastida en_US
dc.subject Leishmania Major en_US
dc.subject Membrane Protein en_US
dc.subject Membrane Surface en_US
dc.subject Mitochondrial Membrane en_US
dc.subject Molecular Biology en_US
dc.subject Molecular Recognition en_US
dc.subject Orthologues en_US
dc.subject Outer Mitochondrial Membranes en_US
dc.subject Peripheral Membranes en_US
dc.subject Protein Cross Linking en_US
dc.subject Protein Folding en_US
dc.subject Protein Structure Tertiary en_US
dc.subject Small Hydrophilic Endoplasmic Reticulum Associated Protein en_US
dc.subject Structural Basis en_US
dc.subject Transgenics en_US
dc.subject Vacuolar Proton-Translocating Atpases en_US
dc.subject Vector Transmission en_US
dc.title Structural basis of molecular recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at membrane surfaces en_US
dc.type info:eu-repo/semantics/article
dc.identifier.doi https://doi.org/10.1074/jbc.M110.130427
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#3.01.00
dc.relation.issn 1083-351X


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