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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

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Type II cadherin ectodomain structures: implications for classical cadherin specificity.

Saurabh D Patel¹, Carlo Ciatto, Chien Peter Chen

¹Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

|March 28, 2006

Summary

This summary is machine-generated.

Classical cadherins (Type I and II) mediate cell adhesion. Structural analysis reveals unique adhesive interfaces in Type II cadherins, driven by swapped beta strands and conserved tryptophan residues, dictating cell specificity.

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Area of Science:

Cellular biology
Structural biology
Biochemistry

Background:

Classical cadherins (Type I and II) are crucial cell adhesion molecules.
Their extracellular domains determine cell-cell recognition and specificity.

Purpose of the Study:

To elucidate the structural basis of cell adhesion specificity in Type II classical cadherins.
To compare the adhesive interfaces of Type I and Type II cadherins.

Main Methods:

Crystal structure determination of ectodomain regions from three Type II cadherins.
Analysis of protein interfaces and conserved residues.
In vitro and in vivo functional assays using chimeric cadherins.

Main Results:

Type II cadherins form adhesive dimers via swapped N-terminal beta strands in their extracellular cadherin-1 (EC1) domains.
These interfaces feature two conserved tryptophan residues and unique hydrophobic regions, distinct from Type I cadherins.
EC1 domains of both Type I and Type II cadherins dictate cell adhesive specificity in vitro.
Chimeric cadherin experiments demonstrate EC1 domain identity is critical for Type II cadherin function in motor neuron segregation in vivo.

Conclusions:

The EC1 domain, particularly its structurally defined adhesive interface, encodes functional specificity for Type II cadherins in vivo.
Structural differences in the EC1 domain interfaces contribute to the distinct adhesive properties of Type I and Type II cadherins.