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Article

ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization.

Molecular biology of the cell - 1 Sept 2002

Boman Annette L, Salo Paul D, Hauglund Melissa J, Strand Nicole L, Rensink Shelly J, Zhdankina Olga

Abstract excerpt

Golgi-localized gamma-ear homology domain, ADP-ribosylation factor (ARF)-binding proteins (GGAs) facilitate distinct steps of post-Golgi traffic. Human and yeast GGA proteins are only ~25% identical, but all GGA proteins have four similar domains based on function and sequence homology. GGA proteins are most conserved in the region that interacts with ARF proteins. To analyze the role of ARF in GGA protein...

Topics

ADP-Ribosylation Factors
Adaptor Proteins, Vesicular Transport
Amino Acid Sequence
Animals
Carrier Proteins
Chromatography, Affinity
Genotype
Glutathione Transferase
Green Fluorescent Proteins
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Immunoblotting

Luminescent Proteins

Microscopy, Fluorescence

Molecular Sequence Data

Mutation

Phenotype

Plasmids

Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 12221117
DOI: 10.1091/mbc.e02-02-0078
PMCID: PMC124144

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ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization.PMID 12221117Read ↗

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