GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23 (Q28143515)

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J B Helms

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J Brunner

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F T Wieland

Journal of Biological Chemistry

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language of work or name

English

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publication date

14 May 1999

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published in

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volume

274

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issue

20

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page(s)

14198-203

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cites work

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Protein sorting by transport vesicles

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ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes

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Coatomer interaction with di-lysine endoplasmic reticulum retention motifs

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A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding

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Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway

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A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer

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An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding

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Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta

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ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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ADP-ribosylation factor 1 transiently activates high-affinity adaptor protein complex AP-1 binding sites on Golgi membranes

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ADP ribosylation factor regulates spectrin binding to the Golgi complex

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Myristoylation of ADP-ribosylation factor 1 facilitates nucleotide exchange at physiological Mg2+ levels

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