P120-Catenin Regulates Early Trafficking Stages of the N-Cadherin Precursor Complex

It is well established that binding of p120 catenin to the cytoplasmic domain of surface cadherin prevents cadherin endocytosis and degradation, contributing to cell-cell adhesion. In the present work we show that p120 catenin bound to the N-cadherin precursor, contributes to its anterograde movemen...

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Bibliographic Details
Published in:PloS one 2016-06, Vol.11 (6), p.e0156758-e0156758
Main Authors: Wehrendt, Diana P, Carmona, Fernando, González Wusener, Ana E, González, Ángela, Martínez, Juan M Lázaro, Arregui, Carlos O
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Binding
Biology and Life Sciences
Cadherin
Cadherins
Cadherins - metabolism
Catenin
Catenins - metabolism
Cell adhesion
Cell junctions
Cell surface
Endocytosis
Endoplasmic reticulum
Ethylmaleimide
Gene Knockdown Techniques
Genetic aspects
Golgi cells
HeLa Cells
Humans
Isoforms
Localization
Models, Biological
N-Cadherin
N-Ethylmaleimide
N-Ethylmaleimide-Sensitive Proteins - metabolism
Physiological aspects
Precursors
Protein Binding
Protein Processing, Post-Translational
Protein Transport
Protein-tyrosine-phosphatase
Recruitment
Research and analysis methods
Secretory Pathway
Tyrosine
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Summary:It is well established that binding of p120 catenin to the cytoplasmic domain of surface cadherin prevents cadherin endocytosis and degradation, contributing to cell-cell adhesion. In the present work we show that p120 catenin bound to the N-cadherin precursor, contributes to its anterograde movement from the endoplasmic reticulum (ER) to the Golgi complex. In HeLa cells, depletion of p120 expression, or blocking its binding to N-cadherin, increased the accumulation of the precursor in the ER, while it decreased the localization of mature N-cadherin at intercellular junctions. Reconstitution experiments in p120-deficient SW48 cells with all three major isoforms of p120 (1, 3 and 4) had similar capacity to promote the processing of the N-cadherin precursor to the mature form, and its localization at cell-cell junctions. P120 catenin and protein tyrosine phosphatase PTP1B facilitated the recruitment of the N-ethylmaleimide sensitive factor (NSF), an ATPase involved in vesicular trafficking, to the N-cadherin precursor complex. Dominant negative NSF E329Q impaired N-cadherin trafficking, maturation and localization at cell-cell junctions. Our results uncover a new role for p120 catenin bound to the N-cadherin precursor ensuring its trafficking through the biosynthetic pathway towards the cell surface.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0156758