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A bipartite signal regulates the faithful delivery of apical domain marker podocalyxin/Gp135.


ABSTRACT: Podocalyxin/Gp135 was recently demonstrated to participate in the formation of a preapical complex to set up initial polarity in MDCK cells, a function presumably depending on the apical targeting of Gp135. We show that correct apical sorting of Gp135 depends on a bipartite signal composed of an extracellular O-glycosylation-rich region and the intracellular PDZ domain-binding motif. The function of this PDZ-binding motif could be substituted with a fusion construct of Gp135 with Ezrin-binding phosphoprotein 50 (EBP50). In accordance with this observation, EBP50 binds to newly synthesized Gp135 at the Golgi apparatus and facilitates oligomerization and sorting of Gp135 into a clustering complex. A defective connection between Gp135 and EBP50 or EBP50 knockdown results in a delayed exit from the detergent-resistant microdomain, failure of oligomerization, and basolateral missorting of Gp135. Furthermore, the basolaterally missorted EBP50-binding defective mutant of Gp135 was rapidly retrieved via a PKC-dependent mechanism. According to these findings, we propose a model by which a highly negative charged transmembrane protein could be packed into an apical sorting platform with the aid of its cytoplasmic partner EBP50.

SUBMITTER: Yu CY 

PROVIDER: S-EPMC1855014 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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A bipartite signal regulates the faithful delivery of apical domain marker podocalyxin/Gp135.

Yu Chun-Ying CY   Chen Jen-Yau JY   Lin Yu-Yu YY   Shen Kuo-Fang KF   Lin Wei-Ling WL   Chien Chung-Liang CL   ter Beest Martin B A MB   Jou Tzuu-Shuh TS  

Molecular biology of the cell 20070301 5


Podocalyxin/Gp135 was recently demonstrated to participate in the formation of a preapical complex to set up initial polarity in MDCK cells, a function presumably depending on the apical targeting of Gp135. We show that correct apical sorting of Gp135 depends on a bipartite signal composed of an extracellular O-glycosylation-rich region and the intracellular PDZ domain-binding motif. The function of this PDZ-binding motif could be substituted with a fusion construct of Gp135 with Ezrin-binding p  ...[more]

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