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Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins |
 | | In addition, certain vacuolar enzymes, notably carboxypeptidase S (Cps1) and the polyphosphatase Ppn1/Phm5, are synthesised as precursors containing a transmembrane domain (TMD) and a short N-terminal cytoplasmic extension that becomes ubiquitinated, directing the proteins to the MVB pathway (Katzmann et al, 2001; Reggiori and Pelham, 2001). |
 | | The markers were green fluorescent protein (GFP)-tagged versions of Cps1, Phm5 and Pep3D, a derivative of Pep12 with a glutamate residue at position 3 of the TMD, which we have previously characterised as a Tul1 substrate. |
 | | Introduction of the Cps1 TMD induced MVB sorting, and this was reduced in both tul1 and bsd2 mutants (Figure 6B). |
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