Cadherins in Brain Morphogenesis and Wiring

Hirano, Shinji; Takeichi, Masatoshi

doi:10.1152/physrev.00014.2011

Cited by 265 publications

(335 citation statements)

References 405 publications

(392 reference statements)

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“…β-Catenin plays an important role in generating the cadherin-dependent adhesive force (30), and it is known to be destabilized by phosphorylation of the serine/ threonine residues at positions 29, 33, 37, 41, and 45 (31,32). Deletion of a segment that included these sites (amino acids 29-48 of β-catenin) results in the stabilization of β-catenin proteins (33).…”

Section: Resultsmentioning

confidence: 99%

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Reelin transiently promotes N-cadherin–dependent neuronal adhesion during mouse cortical development

Matsunaga

Noda

Murakawa

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Reelin is an essential glycoprotein for the establishment of the highly organized six-layered structure of neurons of the mammalian neocortex. Although the role of Reelin in the control of neuronal migration has been extensively studied at the molecular level, the mechanisms underlying Reelin-dependent neuronal layer organization are not yet fully understood. In this study, we directly showed that Reelin promotes adhesion among dissociated neocortical neurons in culture. The Reelin-mediated neuronal aggregation occurs in an N-cadherin-dependent manner, both in vivo and in vitro. Unexpectedly, however, in a rotation culture of dissociated neocortical cells that gradually reaggregated over time, we found that it was the neural progenitor cells [radial glial cells (RGCs)], rather than the neurons, that tended to form clusters in the presence of Reelin. Mathematical modeling suggested that this clustering of RGCs could be recapitulated if the Reelin-dependent promotion of neuronal adhesion were to occur only transiently. Thus, we directly measured the adhesive force between neurons and N-cadherin by atomic force microscopy, and found that Reelin indeed enhanced the adhesiveness of neurons to N-cadherin; this enhanced adhesiveness began to be observed at 30 min after Reelin stimulation, but declined by 3 h. These results suggest that Reelin transiently (and not persistently) promotes N-cadherin-mediated neuronal aggregation. When N-cadherin and stabilized β-catenin were overexpressed in the migrating neurons, the transfected neurons were abnormally distributed in the superficial region of the neocortex, suggesting that appropriate regulation of N-cadherin-mediated adhesion is important for correct positioning of the neurons during neocortical development.T he mammalian neocortex is highly organized into six neuronal layers. This laminar structure is responsible for the complex motor, sensory, and cognitive functions of the mammalian brain (1). Neuronal migration plays an important role in the establishment of this layered structure. Cortical neurons are generated within the ventricular zone (VZ) or subventricular zone (SVZ), and migrate along radial fibers toward the pial surface. Newly born excitatory neurons migrate radially into the cortical plate (CP) past the neurons born earlier, resulting in a birth date-dependent "inside-out" alignment of the neurons in the CP (2-4).Reelin is a glycoprotein that is secreted by the Cajal-Retzius cells in the marginal zone (MZ) of the cortex during neocortical development (5-7). This glycoprotein is essential for establishment of the aforementioned birth date-dependent layered structure of the neocortex, because the CP neurons show an almost inverted alignment in the neocortex of the Reelindeficient, reeler mice. In addition, neurons born at the same time tend to be distributed broadly and not to form clear layers in the reeler cortex (8, 9). Although extensive studies, including at the molecular level, have been conducted to determine the role of Reelin in neuronal migration i...

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Section: Resultsmentioning

confidence: 99%

“…The cytoplasmic domain of N-cadherin is known to play an important role in generating the adhesive force through interaction with β-catenin and p120 catenin (30). β-Catenin has a key role in the formation of adherens junctions through its interactions with cadherin and α-catenin (35).…”

Section: Discussionmentioning

confidence: 99%

Reelin transiently promotes N-cadherin–dependent neuronal adhesion during mouse cortical development

Matsunaga

Noda

Murakawa

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…Catenins are accepted as the primary intracellular mediators of cadherin signaling although other signaling mechanisms have been reported. [5][6][7][8] For comparison, other members of the cadherin superfamily, including the protocadherins, do not bind catenins. 21 Mammalian cadherins can be further subdivided into type I and type II based on sequence homology in the first EC domain; a domain critical for trans-cellular cadherin-cadherin binding 3,33,34 (Fig.…”

Section: The Classic Cadherinsmentioning

confidence: 99%

The classic cadherins in synaptic specificity

Basu

Taylor

Williams

2015

Cell Adhesion & Migration

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“…The cytoplasmic domain is essential in both signal transduction and strengthening of intercellular junctions by virtue of cytoskeletal involvement (Niessen et al, 2011;Saito et al, 2012;van Roy and Berx, 2008). Numerous proteins interact specifically with these cytoplasmic cadherin domains (see Hirano and Takeichi, 2012;Niessen et al, 2011). A central armadillo domain is found in two principal interacting proteins: p120 catenin (p120ctn), which binds to a juxtamembranous conserved cadherin motif; and b-catenin, which binds to a C-terminal conserved cadherin motif.…”

Section: Role Of Catenins In Stem Cell Biologymentioning

confidence: 99%

Role of cell–cell adhesion complexes in embryonic stem cell biology

Pieters

Roy

2014

Journal of Cell Science

121

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Pluripotent embryonic stem cells (ESCs) can self-renew or differentiate into any cell type within an organism. Here, we focus on the roles of cadherins and catenins -their cytoplasmic scaffold proteins -in the fate, maintenance and differentiation of mammalian ESCs. E-cadherin is a master stem cell regulator that is required for both mouse ESC (mESC) maintenance and differentiation. Ecadherin interacts with key components of the naive stemness pathway and ablating it prevents stem cells from forming welldifferentiated teratomas or contributing to chimeric animals. In addition, depleting E-cadherin converts naive mouse ESCs into primed epiblast-like stem cells (EpiSCs). In line with this, a mesenchymal-to-epithelial transition (MET) occurs during reprogramming of somatic cells towards induced pluripotent stem cells (iPSCs), leading to downregulation of N-cadherin and acquisition of high E-cadherin levels. b-catenin exerts a dual function; it acts in cadherin-based adhesion and in WNT signaling and, although WNT signaling is important for stemness, the adhesive function of b-catenin might be crucial for maintaining the naive state of stem cells. In addition, evidence is rising that other junctional proteins are also important in ESC biology. Thus, precisely regulated levels and activities of several junctional proteins, in particular E-cadherin, safeguard naive pluripotency and are a prerequisite for complete somatic cell reprogramming.

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Cadherins in Brain Morphogenesis and Wiring

Cited by 265 publications

References 405 publications

Reelin transiently promotes N-cadherin–dependent neuronal adhesion during mouse cortical development

Reelin transiently promotes N-cadherin–dependent neuronal adhesion during mouse cortical development

The classic cadherins in synaptic specificity

Role of cell–cell adhesion complexes in embryonic stem cell biology

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