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Vol. 9, Issue 12, 3493-3503, December 1998
*Department of Molecular Biology, Graduate School of Medical
Science, Kyushu University, Fukuoka 812-8582, Japan; and
§Molecular Membrane Biology Laboratory, RIKEN (The
Institute of Physical and Chemical Research), Wako, Saitama 351-0198, Japan
To examine the possibility of active recycling of Emp24p between
the endoplasmic reticulum (ER) and the Golgi, we sought to identify
transport signal(s) in the carboxyl-terminal region of Emp24p. Reporter
molecules were constructed by replacing parts of a control
invertase-Wbp1p chimera with those of Emp24p, and their transport rates
were assessed. The transport of the reporter was found to be
accelerated by the presence of the cytoplasmic domain of Emp24p.
Mutational analyses revealed that the two carboxyl-terminal residues,
leucine and valine (LV), were necessary and sufficient to accelerate
the transport. The acceleration was sequence specific, and the terminal
valine appeared to be more important. The LV residues accelerated not
only the overall transport to the vacuole but also the ER to
cis-Golgi transport, suggesting its function in the ER
export. Hence the LV residues are a novel anterograde transport signal.
The double-phenylalanine residues did not affect the transport by
itself but attenuated the effect of the anterograde transport signal.
On the other hand, the transmembrane domain significantly slowed down
the ER to cis-Golgi transport and effectively counteracted
the anterograde transport signal at this step. It may also take part in
the retrieval of the protein, because the overall transport to the
vacuole was more evidently slowed down. Consistently, the mutation of a
conserved glutamine residue in the transmembrane domain further slowed
down the transport in a step after arriving at the
cis-Golgi. Taken together, the existence of the anterograde
transport signal and the elements that regulate its function support
the active recycling of Emp24p.
These authors contributed equally to this work.
Present address: Department of Mycology, Nippon
Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247-0063, Japan.
Corresponding author. E-mail address:
mihara{at}cell.med.kyushu-u.ac.jp.
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