Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface

Clare E. Futter, Christopher N. Connolly, Daniel F. Cutler, Colin R. Hopkins

    Research output: Contribution to journalArticle

    148 Citations (Scopus)

    Abstract

    It is well established that a proportion of newly synthesized lysosomal enzymes and class II major histocompatibility complex antigens are delivered directly to the endocytic pathway from the Golgi complex. Here we show that a significant proportion of newly synthesized transferrin receptors can be detected in endosomes before reaching the cell surface. These newly synthesized transferrin receptors are delivered to the endosome more efficiently than either constitutively secreted soluble proteins or glycophosphatidylinositol-anchored plasma membrane proteins suggesting that their transfer to the endosome is signal-dependent. Identification of a signal-dependent transfer step for proteins like the transferrin receptor operating on the exocytic pathway has important implications for membrane biogenesis, especially in the establishment of cell surface polarity.

    Original languageEnglish
    Pages (from-to)10999-11003
    Number of pages5
    JournalJournal of Biological Chemistry
    Volume270
    Issue number18
    DOIs
    Publication statusPublished - 5 May 1995

    Cite this

    @article{e8e588fbabab49ad938a64e2e66cf214,
    title = "Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface",
    abstract = "It is well established that a proportion of newly synthesized lysosomal enzymes and class II major histocompatibility complex antigens are delivered directly to the endocytic pathway from the Golgi complex. Here we show that a significant proportion of newly synthesized transferrin receptors can be detected in endosomes before reaching the cell surface. These newly synthesized transferrin receptors are delivered to the endosome more efficiently than either constitutively secreted soluble proteins or glycophosphatidylinositol-anchored plasma membrane proteins suggesting that their transfer to the endosome is signal-dependent. Identification of a signal-dependent transfer step for proteins like the transferrin receptor operating on the exocytic pathway has important implications for membrane biogenesis, especially in the establishment of cell surface polarity.",
    author = "Futter, {Clare E.} and Connolly, {Christopher N.} and Cutler, {Daniel F.} and Hopkins, {Colin R.}",
    year = "1995",
    month = "5",
    day = "5",
    doi = "10.1074/jbc.270.18.10999",
    language = "English",
    volume = "270",
    pages = "10999--11003",
    journal = "Journal of Biological Chemistry",
    issn = "0021-9258",
    publisher = "American Society for Biochemistry and Molecular Biology",
    number = "18",

    }

    Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. / Futter, Clare E.; Connolly, Christopher N. ; Cutler, Daniel F.; Hopkins, Colin R.

    In: Journal of Biological Chemistry, Vol. 270, No. 18, 05.05.1995, p. 10999-11003.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface

    AU - Futter, Clare E.

    AU - Connolly, Christopher N.

    AU - Cutler, Daniel F.

    AU - Hopkins, Colin R.

    PY - 1995/5/5

    Y1 - 1995/5/5

    N2 - It is well established that a proportion of newly synthesized lysosomal enzymes and class II major histocompatibility complex antigens are delivered directly to the endocytic pathway from the Golgi complex. Here we show that a significant proportion of newly synthesized transferrin receptors can be detected in endosomes before reaching the cell surface. These newly synthesized transferrin receptors are delivered to the endosome more efficiently than either constitutively secreted soluble proteins or glycophosphatidylinositol-anchored plasma membrane proteins suggesting that their transfer to the endosome is signal-dependent. Identification of a signal-dependent transfer step for proteins like the transferrin receptor operating on the exocytic pathway has important implications for membrane biogenesis, especially in the establishment of cell surface polarity.

    AB - It is well established that a proportion of newly synthesized lysosomal enzymes and class II major histocompatibility complex antigens are delivered directly to the endocytic pathway from the Golgi complex. Here we show that a significant proportion of newly synthesized transferrin receptors can be detected in endosomes before reaching the cell surface. These newly synthesized transferrin receptors are delivered to the endosome more efficiently than either constitutively secreted soluble proteins or glycophosphatidylinositol-anchored plasma membrane proteins suggesting that their transfer to the endosome is signal-dependent. Identification of a signal-dependent transfer step for proteins like the transferrin receptor operating on the exocytic pathway has important implications for membrane biogenesis, especially in the establishment of cell surface polarity.

    U2 - 10.1074/jbc.270.18.10999

    DO - 10.1074/jbc.270.18.10999

    M3 - Article

    VL - 270

    SP - 10999

    EP - 11003

    JO - Journal of Biological Chemistry

    JF - Journal of Biological Chemistry

    SN - 0021-9258

    IS - 18

    ER -