UNIGE document Doctoral Thesis
previous document  unige:18035  next document
add to browser collection
Title

Molecular interactions and junctional recruitment of paracingulin : identification and characterization of a new adherens junction protein, PLEKHA7
Author
Pulimeno, Pamela
Directors
Gonzalez Gaitan, Marcos
Citi, Sandra
Defense Thèse de doctorat : Univ. Genève, 2011 - Sc. 4364 - 2011/10/18
Abstract Epithelial cells are characterized by a junctional complex, which consists of tight junctions (TJ), adherens junctions (AJ) and desmosomes (D). The junctional complex is formed by both integral membrane proteins, which allow adhesion and form a paracellular barrier, and cytoplasmic proteins, which connect transmembrane proteins to the cytoskeleton and have signalling functions. Understanding how the junctional complex is assembled and regulated is of fundamental importance for epithelial physiology. Paracingulin is a cytoplasmic protein of TJ and AJ, which regulates the activity of small GTPases, RhoA and Rac1. In this work we characterize the molecular interactions of paracingulin at epithelial junctions, and show that paracingulin forms a complex with ZO-1, cingulin, E-cadherin, PLEKHA7 and p120ctn. We provide the first characterization of expression and tissue distribution of PLEKHA7, a paracingulin-binding protein, and we demonstrate that PLEKHA7 recruits paracingulin to AJ, whereas ZO-1 targets paracingulin to TJ.
Keywords Epithelial cell — Tight junctions — Adherens junction — Paracingulin — Cingulin — PLEKHA7 — ZO-1 — MDCK — Cytoskeleton
Identifiers
URN: urn:nbn:ch:unige-180351
Full text
Thesis (22.3 MB) - document accessible for UNIGE members only Limited access to UNIGE
Structures
Faculté des sciences / Section de biologie / Département de biologie moléculaire
Citation
(ISO format) 		PULIMENO, Pamela. Molecular interactions and junctional recruitment of paracingulin : identification and characterization of a new adherens junction protein, PLEKHA7. Université de Genève. Thèse, 2011. https://archive-ouverte.unige.ch/unige:18035

442 hits

5 downloads

Contact an author

Update request

Update

Deposited on : 2012-01-10

Export document
Format :
Citation style :