Identification and characterization of novel clathrin adaptor-related proteins.
We have identified a human approximately 87-kDa protein, designated as gamma2-adaptin, that is similar to gamma-adaptin (called gamma1-adaptin in this paper), a large chain of the AP-1 clathrin-associated adaptor complex, not only in the primary structure (60% amino acid identity) but also in the domain organization. Northern blot analysis has ... shown that its mRNA is expressed in a variety of tissues. Analysis using a yeast two-hybrid system has revealed that, similarly to gamma1-adaptin, gamma2-adaptin is capable of interacting not only with the sigma1 chain (called as sigma1A in this paper), the small chain of the AP-1 complex, but also with a novel sigma1-like protein, designated as sigma1B, which shows an 87% amino acid identity to sigma1A; and that, unlike gamma1-adaptin, it is unable to interact with beta1-adaptin, another large chain of the AP-1 complex. Immunofluorescence microscopy analysis has revealed that gamma2-adaptin is localized to paranuclear vesicular structures that are not superimposed on structures containing gamma1-adaptin. Furthermore, unlike gamma1-adaptin, gamma2-adaptin is recruited onto membranes in the presence of a fungal antibiotic, brefeldin A. These data suggest that gamma2-adaptin constitute a novel adaptor-related complex that participates in a transport step different from that of AP-1.
Mesh Terms:
Adaptor Protein Complex 1, Adaptor Protein Complex 2, Adaptor Protein Complex alpha Subunits, Adaptor Protein Complex gamma Subunits, Adaptor Protein Complex sigma Subunits, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Base Sequence, Binding Sites, Cell Line, Clathrin, Cloning, Molecular, DNA Primers, Humans, Membrane Proteins, Molecular Sequence Data, Organ Specificity, Polymerase Chain Reaction, RNA, Messenger, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transcription Factor AP-1, Transcription, Genetic, Transfection, Tumor Cells, Cultured
Adaptor Protein Complex 1, Adaptor Protein Complex 2, Adaptor Protein Complex alpha Subunits, Adaptor Protein Complex gamma Subunits, Adaptor Protein Complex sigma Subunits, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Base Sequence, Binding Sites, Cell Line, Clathrin, Cloning, Molecular, DNA Primers, Humans, Membrane Proteins, Molecular Sequence Data, Organ Specificity, Polymerase Chain Reaction, RNA, Messenger, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transcription Factor AP-1, Transcription, Genetic, Transfection, Tumor Cells, Cultured
J. Biol. Chem.
Date: Sep. 18, 1998
PubMed ID: 9733768
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