Localization and Trafficking of an Isoform of the AtPRA1 Family to the Golgi Apparatus Depend on Both N- and C-Terminal Sequence Motifs

Prenylated Rab acceptors (PRAs) bind to prenylated Rab proteins and possibly aid in targeting Rabs to their respective compartments. In Arabidopsis, 19 isoforms of PRA1 have been identified and, depending upon the isoforms, they localize to the endoplasmic reticulum (ER), Golgi apparatus and endosom...

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Bibliographic Details
Published in:Traffic (Copenhagen, Denmark) Denmark), 2011-02, Vol.12 (2), p.185-200
Main Authors: Jung, Chan Jin, Hui Lee, Myoung, Ki Min, Myung, Hwang, Inhwan
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Amino Acid Motifs
Amino Acid Sequence
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
AtPRA1 isoform
Endoplasmic Reticulum - metabolism
ER exit signals
Golgi apparatus
Golgi Apparatus - metabolism
Localization
Membrane Proteins - genetics
Membrane Proteins - metabolism
Molecular Sequence Data
Plants, Genetically Modified
Protein Interaction Domains and Motifs
Protein Isoforms
Protein Prenylation - genetics
Protein Structure, Tertiary
Protein Transport
Protoplasts - metabolism
rab GTP-Binding Proteins - genetics
rab GTP-Binding Proteins - metabolism
Structure-Activity Relationship
trafficking and localization
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Summary:Prenylated Rab acceptors (PRAs) bind to prenylated Rab proteins and possibly aid in targeting Rabs to their respective compartments. In Arabidopsis, 19 isoforms of PRA1 have been identified and, depending upon the isoforms, they localize to the endoplasmic reticulum (ER), Golgi apparatus and endosomes. Here, we investigated the localization and trafficking of AtPRA1.B6, an isoform of the Arabidopsis PRA1 family. In colocalization experiments with various organellar markers, AtPRA1.B6 tagged with hemagglutinin (HA) at the N-terminus localized to the Golgi apparatus in protoplasts and transgenic plants. The valine residue at the C-terminal end and an EEE motif in the C-terminal cytoplasmic domain were critical for anterograde trafficking from the ER to the Golgi apparatus. The N-terminal region contained a sequence motif for retention of AtPRA1.B6 at the Golgi apparatus. In addition, anterograde trafficking of AtPRA1.B6 from the ER to the Golgi apparatus was highly sensitive to the HA:AtPRA1.B6 level. The region that contains the sequence motif for Golgi retention also conferred the abundance-dependent trafficking inhibition. On the basis of these results, we propose that AtPRA1.B6 localizes to the Golgi apparatus and its ER-to-Golgi trafficking and localization to the Golgi apparatus are regulated by multiple sequence motifs in both the C- and N-terminal cytoplasmic domains.
ISSN:1398-9219
1600-0854
DOI:10.1111/j.1600-0854.2010.01140.x