Mechanism of extracellular domain-deleted dominant negative cadherins

1999 ◽  
Vol 112 (10) ◽  
pp. 1621-1632 ◽  
Author(s):  
M.T. Nieman ◽  
J.B. Kim ◽  
K.R. Johnson ◽  
M.J. Wheelock
Keyword(s):  
Embryonic Development ◽  
Family Member ◽  
Mechanism Of Action ◽  
Cultured Cells ◽  
Extracellular Domain ◽  
Cell Interactions ◽  
Dominant Negative ◽  
Single Family ◽  
Dependent Cell ◽  
Cell Cell

The cadherin/catenin complex mediates Ca2+-dependent cell-cell interactions that are essential for normal developmental processes. It has been proposed that sorting of cells during embryonic development is due, at least in part, to expression of different cadherin family members or to expression of differing levels of a single family member. Expression of dominant-negative cadherins has been used experimentally to decrease cell-cell interactions in whole organisms and in cultured cells. In this study, we elucidated the mechanism of action of extracellular domain-deleted dominant-negative cadherin, showing that it is not cadherin isotype-specific, and that it must be membrane-associated but the orientation within the membrane does not matter. In addition, membrane-targeted cytoplasmic domain cadherin with the catenin-binding domain deleted does not function as a dominant-negative cadherin. Expression of extracellular domain-deleted dominant-negative cadherin results in down-regulation of endogenous cadherins which presumably contributes to the non-adhesive phenotype.

scholarly journals PH-dependent cell–cell interactions in the green alga Chara

PROTOPLASMA ◽  
2019 ◽  
Vol 256 (6) ◽  
pp. 1737-1751
Author(s):  
Alexey Eremin ◽  
Alexander A. Bulychev ◽  
Christopher Kluge ◽  
Jeremy Harbinson ◽  
Ilse Foissner
Keyword(s):  
Green Alga ◽  
Cell Interactions ◽  
Dependent Cell ◽  
Ph Dependent ◽  
Cell Cell

scholarly journals Cell-Cell Interactions Influence Vascular Reprogramming by Prox1 during Embryonic Development

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e52197 ◽  
Author(s):  
Harold Kim ◽  
Maribelle Cruz ◽  
Annie Bourdeau ◽  
Daniel J. Dumont
Keyword(s):  
Embryonic Development ◽  
Cell Interactions ◽  
Cell Cell

Robo2-Slit1 dependent cell-cell interactions mediate assembly of the trigeminal ganglion

2008 ◽  
Vol 11 (3) ◽  
pp. 269-276 ◽  
Author(s):  
Celia E Shiau ◽  
Peter Y Lwigale ◽  
Raman M Das ◽  
Stuart A Wilson ◽  
Marianne Bronner-Fraser
Keyword(s):  
Trigeminal Ganglion ◽  
Cell Interactions ◽  
Dependent Cell ◽  
Cell Cell

scholarly journals A modular microfluidic bioreactor to investigate plant cell–cell interactions

PROTOPLASMA ◽  
2021 ◽  
Author(s):  
T. Finkbeiner ◽  
C. Manz ◽  
M. L. Raorane ◽  
C. Metzger ◽  
L. Schmidt-Speicher ◽  
...  
Keyword(s):  
Plant Cell ◽  
Cell Biology ◽  
Cultured Cells ◽  
Abiotic Factors ◽  
Welding Process ◽  
Cell Types ◽  
Cell Interactions ◽  
Chemical Signalling ◽  
Different Cell Types ◽  
Cell Cell

AbstractPlants produce a wide variety of secondary metabolites, which often are of interest to pharmaceutical and nutraceutical industry. Plant-cell cultures allow producing these metabolites in a standardised manner, independently from various biotic and abiotic factors difficult to control during conventional cultivation. However, plant-cell fermentation proves to be very difficult, since these chemically complex compounds often result from the interaction of different biosynthetic pathways operating in different cell types. To simulate such interactions in cultured cells is a challenge. Here, we present a microfluidic bioreactor for plant-cell cultivation to mimic the cell–cell interactions occurring in real plant tissues. In a modular set-up of several microfluidic bioreactors, different cell types can connect through a flow that transports signals or metabolites from module to module. The fabrication of the chip includes hot embossing of a polycarbonate housing and subsequent integration of a porous membrane and in-plane tube fittings in a two-step ultrasonic welding process. The resulting microfluidic chip is biocompatible and transparent. Simulation of mass transfer for the nutrient sucrose predicts a sufficient nutrient supply through the membrane. We demonstrate the potential of this chip for plant cell biology in three proof-of-concept applications. First, we use the chip to show that tobacco BY-2 cells in suspension divide depending on a “quorum-sensing factor” secreted by proliferating cells. Second, we show that a combination of two Catharanthus roseus cell strains with complementary metabolic potency allows obtaining vindoline, a precursor of the anti-tumour compound vincristine. Third, we extend the approach to operationalise secretion of phytotoxins by the fungus Neofusicoccum parvum as a step towards systems to screen for interorganismal chemical signalling.

SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling

Development ◽  
1997 ◽  
Vol 124 (23) ◽  
pp. 4759-4767 ◽  
Author(s):  
C. Wen ◽  
M.M. Metzstein ◽  
I. Greenwald
Keyword(s):  
Caenorhabditis Elegans ◽  
Genetic Analysis ◽  
Extracellular Domain ◽  
Notch Signalling ◽  
Cell Interactions ◽  
Cell Fates ◽  
Cell Ablation ◽  
Adam Family ◽  
Mediate Cell ◽  
Cell Cell

LIN-12/NOTCH proteins mediate cell-cell interactions that specify cell fates. Previous work suggested that sup-17 facilitates lin-12 signalling in Caenorhabditis elegans. Here, we show that sup-17 encodes a member of the ADAM family of metalloproteases. SUP-17 is highly similar to Drosophila KUZBANIAN, which functions in Drosophila neurogenesis, and the vertebrate ADAM10 protein. Furthermore, we show by genetic analysis that the extracellular domain of LIN-12 appears to be necessary for sup-17 to facilitate lin-12 signalling and that sup-17 does not act downstream of lin-12. Finally, we show by cell ablation experiments that sup-17 can act cell autonomously to facilitate lin-12 activity. We discuss the implications of our observations for LIN-12/NOTCH signalling and how our results complement and extend results obtained from genetic analysis of kuz in Drosophila.

N-cadherin in adult rat cardiomyocytes in culture. I. Functional role of N-cadherin and impairment of cell-cell contact by a truncated N-cadherin mutant

1996 ◽  
Vol 109 (1) ◽  
pp. 1-10 ◽  
Author(s):  
C.M. Hertig ◽  
M. Eppenberger-Eberhardt ◽  
S. Koch ◽  
H.M. Eppenberger
Keyword(s):  
Ectopic Expression ◽  
Extracellular Domain ◽  
Large Deletion ◽  
Binding Domain ◽  
Dominant Negative ◽  
Cell Contact ◽  
Rat Cardiomyocytes ◽  
Cell Contacts ◽  
Adult Rat ◽  
Cell Cell

N-cadherin is a transmembrane Ca(2+)-dependent glycoprotein that is part of adherens junctions. It functions with the cell adhesion N-terminal extracellular domain as a site of homophilic cell-cell contacts. The intracellular C-terminal domain provides via a catenin complex the interaction with the cytoskeleton. Ectopic expression of chicken N-cadherin in adult rat cardiomyocytes (ARC) in culture was obtained after microinjection into non-dividing cardiomyocytes; it was demonstrated that the exogenous protein colocalized with the endogenous N-cadherin at the plasma membrane of the cell and formed contact sites. A dominant negative chicken N-cadherin mutant was constructed by a large deletion of the extracellular domain. This mutant was expressed and inhibited the function of the endogenous rat N-cadherin probably by competing for the catenin complex binding domain, which is essential for the formation of a stable cell-cell contact of ARC. The injected cells lost contact with neighbouring cells and retracted; the connexons of the gap junctions were pulled out as well. This could be avoided by another N-cadherin mutation, which, in addition to the N-terminal truncation, contained a deletion of the catenin binding domain. In the case of the truncated N-cadherin at the N terminus, the sarcomeric structure of the myofibrils of ARC was also affected. Myofibrils were the most vulnerable cytoskeletal structures affected by the overexpressed dominant negative N-cadherin mutation. Similar behaviour was shown when cardiomyocytes separated following Ca2+ depletion and when new cell-cell contacts were formed after Ca2+ replenishment. N-cadherin is thought to be the essential component for establishing new cell-cell contacts which eventually led to a new formation of intercalated disc-like structures in the cardiac cell culture.

Function and specificity of LIM domains in Drosophila nervous system and wing development

Development ◽  
1998 ◽  
Vol 125 (19) ◽  
pp. 3915-3923 ◽  
Author(s):  
D.D. O'Keefe ◽  
S. Thor ◽  
J.B. Thomas
Keyword(s):  
Nervous System ◽  
Family Member ◽  
Protein Interactions ◽  
Gene Selection ◽  
Cultured Cells ◽  
Nervous System Development ◽  
Dominant Negative ◽  
Lim Domains

LIM domains are found in a variety of proteins, including cytoplasmic and nuclear LIM-only proteins, LIM-homeodomain (LIM-HD) transcription factors and LIM-kinases. Although the ability of LIM domains to interact with other proteins has been clearly established in vitro and in cultured cells, their in vivo function is unknown. Here we use Drosophila to test the roles of the LIM domains of the LIM-HD family member Apterous (Ap) in wing and nervous system development. Using a rescuing assay of the ap mutant phenotype, we have found that the LIM domains are essential for Ap function. Furthermore, expression of LIM domains alone can act in a dominant-negative fashion to disrupt Ap function. The Ap LIM domains can be replaced by those of another family member to generate normal wing structure, but LIM domains are not interchangeable during axon pathfinding of the Ap neurons. This suggests that the Ap LIM domains mediate different protein interactions in different developmental processes, and that LIM domains can participate in conferring specificity of target gene selection.

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