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Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands.

Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Research Abstract Details 

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  • Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Abstract Text:

    k ozakiK Ozaki,n itohN Itoh,t kawasakiT Kawasaki,

    A macrophage asialoglycoprotein binding protein (M-ASGP-BP), which is an endocytic receptor specific for Gal/GalNAc-terminated glycoproteins, was shown to be functionally active as a homooligomer (hexamer or octamer) of a single polypeptide chain of 42 kDa [Ozaki, K., Ii, M., Itoh, N., & Kawasaki, T. (1992) J. Biol. Chem. 267, 9229-9235]. In various endocytic receptors, a four-amino-acid sequence, Tyr-X-Y-Phe, in the cytoplasmic domain has been identified as an internalization signal [Pearse, B.M.F. & Robinson, M.S. (1990) Annu. Rev. Cell Biol. 265, 151-171]. The amino-terminus of the M-ASGP-BP deduced from its cDNA sequence was found to contain the sequence, Tyr5-Glu6-Asn7-Phe8, in its cytoplasmic tail. This was confirmed by the fact that the recombinant M-ASGP-BP isolated from transfected COS-1 cells was found to have the amino-terminal sequence, Thr2-Met3-Ala4-Tyr5-Glu6-Asn7-Phe8. The role of this presumptive internalization signal in the cytoplasmic tail was studied by measuring the endocytic activity of the wild-type and mutant M-ASGP-BPs expressed on COS-1 cells through transfection with the wild-type and mutant cDNAs prepared by oligonucleotide-directed mutagenesis, respectively. On the deletion of Tyr5 or replacement of it with alanine, the internalization of asialoorosomucoid (ASOR) decreased to approximately one-fourth that in the case of the wild-type molecule. On replacement of Tyr5 with phenylalanine, the internalization proceeded at a rate similar to that in the case of the wild-type molecule.(ABSTRACT TRUNCATED AT 250 WORDS)

    Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Publishing Authors By Initials

    k ozakiK Ozaki,n itohN Itoh,t kawasakiT Kawasaki,

    For similar amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research

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    Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 113

    Page Numbers: 271-6

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Mar

    YEAR: 1993

    Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Keywords Mesh Terms:

    KEYWORDS: Tyrosine

    MESH TERMS: physiology

    Chemical & Substance for Abstract: Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands. Information

    Substance Name: DNA

    Registry Number: 9007-49-2

    Grant and Affiliation Information for Role of tyrosine-5 in the cytoplasmic tail of the macrophage asialoglycoprotein receptor in the rapid internalization of ligands.

    AFFILIATION: Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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