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The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif

Ritz, A. M. and Trautwein, M. and Grassinger, F. and Spang, A.. (2014) The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif. Cell Reports, 7 (1). pp. 249-260.

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Abstract

Prion and prion-like domains (PLDs) are found in many proteins throughout the animal kingdom. We found that the PLD in the S. cerevisiae exomer-depen- dent cargo protein Pin2 is involved in the regulation of protein transport and localization. The domain serves as a Pin2 retention signal in the trans-Golgi network (TGN). Pin2 is localized in a polarized fashion at the plasma membrane of the bud early in the cell cycle and the bud neck at cytokinesis. This polarized local- ization is dependent on both exo- and endocytosis. Upon environmental stress, Pin2 is rapidly endocy- tosed, and the PLD aggregates and causes seques- tration of Pin2. The aggregation of Pin2 is reversible upon stress removal and Pin2 is rapidly re-exported to the plasma membrane. Altogether, these data un- cover a role for PLDs as protein localization elements.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Spang)
UniBasel Contributors:Spang, Anne
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Elsevier
e-ISSN:2211-1247
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
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Last Modified:05 Oct 2017 09:50
Deposited On:25 Apr 2014 08:01

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