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EMBO reports 9, 12, 1216–1221 (2008)
doi:10.1038/embor.2008.199
AOP Published online: 24 October 2008
Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
EMBO Open
Elina Nikko, James A Sullivan† & Hugh R B Pelham
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MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
To whom correspondence should be addressed
Hugh R B Pelham Tel: +44 (0)1223 402216; Fax: +44 (0)1223 249565; E-mail: hp@mrc-lmb.cam.c.uk
† Present address: School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK
Received 15 September 2008; Accepted 25 September 2008; Published online 24 October 2008.
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Abstract
Many plasma membrane proteins in yeast are ubiquitinated and endocytosed, but how they are recognized for modification has remained unknown. Here, we show that the manganese transporter Smf1 is endocytosed when cells are exposed to cadmium ions, that this endocytosis depends on Rsp5-dependent ubiquitination of specific lysines and that it also requires phosphorylation at nearby sites. This phosphorylation is, however, constitutive rather than stress-induced. Efficient ubiquitination requires Ecm21 or Csr2, two members of a family of arrestin-like yeast proteins that contain several PY motifs and bind to Rsp5. Ecm21 also binds to phosphorylated Smf1, providing a link between Rsp5 and its substrate. PY motif-containing arrestin-like proteins are found in many species, including humans, and might have a general role as ubiquitin ligase adaptors.
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