Abstract
Binding of the receptor-associated protein (RAP) to the newly identified putative sorting receptor, sortilin, was analyzed by surface plasmon resonance analysis of recombinant RAP and sortilin domains and compared with binding to megalin and low density lipoprotein receptor-related protein (LRP). The data show that the RAP-binding site in sortilin is localized in the cysteine-rich lumenal part homologous to yeast vacuolar protein-sorting 10 protein (Vps10p), and the sortilin-binding site in RAP is localized in the carboxy-terminal domain III of the three homologous domains in RAP. Whereas sortilin bound only RAP domain III, megalin and LRP bound all RAP domains with the functional affinity order: domain III >domain I > domain II.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Vesicular Transport
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Animals
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CHO Cells / metabolism
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Cricetinae
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Fungal Proteins / chemistry*
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Heymann Nephritis Antigenic Complex
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / metabolism*
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism*
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Protein Conformation
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Receptors, Cell Surface / chemistry*
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Receptors, LDL / metabolism
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Saccharomyces cerevisiae Proteins*
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Vesicular Transport Proteins*
Substances
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Adaptor Proteins, Vesicular Transport
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Fungal Proteins
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Heymann Nephritis Antigenic Complex
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Membrane Glycoproteins
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Nerve Tissue Proteins
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PEP1 protein, S cerevisiae
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Receptors, Cell Surface
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Receptors, LDL
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Saccharomyces cerevisiae Proteins
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Vesicular Transport Proteins
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sortilin