Endoplasmic Reticulum Retention Signal-Dependent Glycylation of the Hsp70/Grp170-Related Pgp1p in Tetrahymena | Zendy

Rong Xie | Zendy; Kathleen M. Clark | Zendy; Martin A. Gorovsky | Zendy

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Endoplasmic Reticulum Retention Signal-Dependent Glycylation of the Hsp70/Grp170-Related Pgp1p in Tetrahymena

Author(s) -

Rong Xie,

Kathleen M. Clark,

Martin A. Gorovsky

Publication year - 2006

Publication title -

eukaryotic cell

Language(s) - English

Resource type - Journals

eISSN - 1535-9778

pISSN - 1535-9786

DOI - 10.1128/ec.00366-06

Subject(s) - endoplasmic reticulum , tetrahymena , biology , microbiology and biotechnology , glycoprotein , signal peptide , glycosylation , secretory pathway , biochemistry , gene , peptide sequence , golgi apparatus

Glycylation is an uncommon posttranslational modification. It has been found that tubulin glycylation is essential for cell survival inTetrahymena . Here we describePGP1 , aTetrahymena gene encoding an Hsp70 homologue that is a novel glycylated protein. Pgp1p is a conserved glycoprotein that localizes within the lumen of the endoplasmic reticulum (ER). We demonstrate thatPGP1 is essential for viability and present evidence that both glycosylation and ER retention are necessary but not sufficient for glycylation.

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