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PMID:12429846

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Citation

Kalthoff, C, Groos, S, Kohl, R, Mahrhold, S and Ungewickell, EJ (2002) Clint: a novel clathrin-binding ENTH-domain protein at the Golgi. Mol. Biol. Cell 13:4060-73

Abstract

We have characterized a novel clathrin-binding 68-kDa epsin N-terminal homology domain (ENTH-domain) protein that we name clathrin interacting protein localized in the trans-Golgi region (Clint). It localizes predominantly to the Golgi region of epithelial cells as well as to more peripheral vesicular structures. Clint colocalizes with AP-1 and clathrin only in the perinuclear area. Recombinantly expressed Clint interacts directly with the gamma-appendage domain of AP-1, with the clathrin N-terminal domain through the peptide motif (423)LFDLM, with the gamma-adaptin ear homology domain of Golgi-localizing, gamma-adaptin ear homology domain 2, with the appendage domain of beta2-adaptin and to a lesser extent with the appendage domain of alpha-adaptin. Moreover, the Clint ENTH-domain asssociates with phosphoinositide-containing liposomes. A significant amount of Clint copurifies with rat liver clathrin-coated vesicles. In rat kidney it is preferentially expressed in the apical region of epithelial cells that line the collecting duct. Clathrin and Clint also colocalize in the apical region of enterocytes along the villi of the small intestine. Apart from the ENTH-domain Clint has no similarities with the epsins AP180/CALM or Hip1/1R. A notable feature of Clint is a carboxyl-terminal methionine-rich domain (Met(427)-Met(605)), which contains >17% methionine. Our results suggest that Clint might participate in the formation of clathrin-coated vesicles at the level of the trans-Golgi network and remains associated with the vesicles longer than clathrin and adaptors.

Links

PubMed PMC133614 Online version:10.1091/mbc.E02-03-0171

Keywords

Adaptor Protein Complex gamma Subunits/metabolism; Adaptor Proteins, Vesicular Transport; Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins/chemistry; Carrier Proteins/genetics; Cell Fractionation; Cell Line; Clathrin/metabolism; Clathrin-Coated Vesicles/metabolism; Epithelial Cells/cytology; Epithelial Cells/metabolism; Golgi Apparatus/chemistry; Golgi Apparatus/metabolism; Humans; Liposomes/chemistry; Liposomes/metabolism; Male; Models, Molecular; Molecular Sequence Data; Neuropeptides/genetics; Protein Binding; Protein Structure, Tertiary; Rats; Rats, Wistar; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Sequence Alignment; Tissue Distribution; Transcription Factor AP-1/metabolism; Vesicular Transport Proteins

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

BOVIN:EPN4

located_in

GO:0048471: perinuclear region of cytoplasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

BOVIN:EPN4

located_in

GO:0005798: Golgi-associated vesicle

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

BOVIN:EPN4

located_in

GO:0005802: trans-Golgi network

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

PIG:C0MHR2

located_in

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:CLH1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q14677

F

Seeded From UniProt

complete

HUMAN:EPN4

enables

GO:0030276: clathrin binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q00610

F

Seeded From UniProt

complete

HUMAN:EPN4

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9UJY4

F

Seeded From UniProt

complete

HUMAN:GGA2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q14677

F

Seeded From UniProt

complete


See also

References

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