NDLI: SDF2L1, a component of the endoplasmic reticulum chaperone complex, differentially interacts with {alpha}-, {beta}-, and {theta}-defensin propeptides.

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SDF2L1, a component of the endoplasmic reticulum chaperone complex, differentially interacts with {alpha}-, {beta}-, and {theta}-defensin propeptides.

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SDF2L1, a component of the endoplasmic reticulum chaperone complex, differentially interacts with {alpha}-, {beta}-, and {theta}-defensin propeptides.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tongaonkar, Prasad Selsted, Michael E.
Description	Author Affiliation: Tongaonkar P ( Department of Pathology & Laboratory Medicine, School of Medicine, University of California, Irvine, Irvine, California 92697, USA. ptongaon@uci.edu)
Abstract	Mammalian defensins are cationic antimicrobial peptides that play a central role in host innate immunity and as regulators of acquired immunity. In animals, three structural defensin subfamilies, designated as alpha, beta, and , have been characterized, each possessing a distinctive tridisulfide motif. Mature alpha- and beta-defensins are produced by simple proteolytic processing of their prepropeptide precursors. In contrast, the macrocyclic -defensins are formed by the head-to-tail splicing of nonapeptides excised from a pair of prepropeptide precursors. Thus, elucidation of the -defensin biosynthetic pathway provides an opportunity to identify novel factors involved in this unique process. We incorporated the -defensin precursor, proRTD1a, into a bait construct for a yeast two-hybrid screen that identified rhesus macaque stromal cell-derived factor 2-like protein 1 (SDF2L1), as an interactor. SDF2L1 is a component of the endoplasmic reticulum (ER) chaperone complex, which we found to also interact with alpha- and beta-defensins. However, analysis of the SDF2L1 domain requirements for binding of representative alpha-, beta-, and -defensins revealed that alpha- and beta-defensins bind SDF2L1 similarly, but differently from the interactions that mediate binding of SDF2L1 to pro--defensins. Thus, SDF2L1 is a factor involved in processing and/or sorting of all three defensin subfamilies.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	9
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-02-27
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Defensins Metabolism Endoplasmic Reticulum Membrane Proteins Molecular Chaperones Protein Precursors Alpha-Defensins Beta-Defensins Amino Acid Sequence Animals Blotting, Western Bone Marrow Chemistry Genetics Glutathione Transferase HL-60 Cells Immunoprecipitation Macaca Mulatta Molecular Sequence Data Myeloid Cells Protein Biosynthesis Saccharomyces Cerevisiae Growth & Development Sequence Homology, Amino Acid Transcription, Genetic Two-Hybrid System Techniques Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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