A new pathway for protein export in Saccharomyces cerevisiae

doi:10.1083/jcb.133.5.1017

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A new pathway for protein export in Saccharomyces cerevisiae

AE Cleves, DN Cooper, SH Barondes and RB Kelly
Department of Biochemistry and Biophysics, University of California, San Francisco, 94143-0534, USA. cleves@cgl.ucsf.edu

Several physiologically important proteins lack a classical secretory signal sequence, yet they are secreted from cells. To investigate the secretion mechanism of such proteins, a representative mammalian protein that is exported by a nonclassical mechanism, galectin-1, has been expressed in yeast. Galectin-1 is exported across the yeast plasma membrane, and this export does not require the classical secretory pathway nor the yeast multidrug resistance-like protein Ste6p, the transporter for the peptide a factor. A screen for components of the export machinery has identified genes that are involved in nonclassical export. These findings demonstrate a new pathway for protein export that is distinct from the classical secretory pathway in yeast.
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