
doi: 10.1247/csf.10022
pmid: 21368446
SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (-/-) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.
Membrane Glycoproteins, Cell Membrane, Molecular Sequence Data, Gene Expression, Membrane Proteins, Endosomes, Mice, Protein Transport, Viral Envelope Proteins, COS Cells, Chlorocebus aethiops, Mutation, Animals, Humans, Amino Acid Sequence, HeLa Cells, trans-Golgi Network
Membrane Glycoproteins, Cell Membrane, Molecular Sequence Data, Gene Expression, Membrane Proteins, Endosomes, Mice, Protein Transport, Viral Envelope Proteins, COS Cells, Chlorocebus aethiops, Mutation, Animals, Humans, Amino Acid Sequence, HeLa Cells, trans-Golgi Network
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