Abstract
A cellular role and the mechanism of action for small GTPase Arl1 have been defined. Arl1-GTP interacts with the GRIP domains of Golgin-97 and Golgin-245, a process dependent on conserved residues of the GRIP domains that are important for Golgi targeting. The switch II region of Arl1 confers the specificity of this interaction. Arl1-GTP mediates Golgi recruitment of Golgin-97 in a switch II-dependent manner, whereas tethering Arl1-GTP onto endosomes can mediate endosomal targeting of Golgin-97. Golgin-97 and Golgin-245 are dissociated from the Golgi when Arl1 is knocked-down by its siRNA. Arl1-GTP thus functions to recruit Golgin-97 and Golgin-245 onto the Golgi via interacting with their GRIP domains.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ADP-Ribosylation Factors / drug effects
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ADP-Ribosylation Factors / metabolism*
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Amino Acid Sequence
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Autoantigens / metabolism*
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Cells, Cultured
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Cloning, Molecular
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Golgi Matrix Proteins
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Humans
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Membrane Proteins / drug effects
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Peptides / metabolism*
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Protein Binding
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Protein Structure, Tertiary / genetics
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RNA, Small Interfering / pharmacology
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Sequence Analysis, Protein
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Two-Hybrid System Techniques
Substances
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Autoantigens
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Golgi Matrix Proteins
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Golgi complex autoantigen, 97-kDa
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Membrane Proteins
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Peptides
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RNA, Small Interfering
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p 230
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ADP-ribosylation factor related proteins
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ADP-Ribosylation Factors