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MBC in Press, published online ahead of print July 11, 2003
Mol. Biol. Cell 10.1091/mbc.E03-05-0268

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Submitted on May 1, 2003
Revised on June 24, 2003
Accepted on June 24, 2003

Specificity of binding of the plectin Actin Binding Domain to {beta}4 integrin

Sandy H.M. Litjens1, Jan Koster1, Ingrid Kuikman1, Sandra van Wilpe1, José M. de Pereda2, and Arnoud Sonnenberg1*

1 The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
2 Program on Cell adhesion, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037

* Corresponding author. E-mail address: a.sonnenberg{at}nki.nl.

Plectin is a major component of the cytoskeleton and links the intermediate filament system to hemidesmosomes by binding to the integrin {beta}4 subunit. Previously, a binding site for {beta}4 was mapped on the actin-binding domain (ABD) of plectin and binding of {beta}4 and F-actin to plectin was shown to be mutually exclusive. Here we show that only the ABDs of plectin and dystonin bind to {beta}4, whereas those of other actin-binding proteins do not. Mutations of the ABD of plectin-1C show that Q131, R138 and N149 are critical for tight binding of the ABD to {beta}4. These residues form a small cavity, occupied by a well-ordered water molecule in the crystal structure. The {beta}4 binding pocket partly overlaps with the actin-binding sequence 2 (ABS2), previously shown to be essential for actin binding. Therefore, steric interference may render binding of F-actin and {beta}4 to plectin mutually exclusive. Finally, we provide evidence indicating that the residues preceding the ABD in plectin-1A and -1C, although unable to mediate binding to {beta}4 themselves, modulate the binding activity of the ABD for {beta}4. These studies demonstrate the unique property of the plectin-ABD to bind to both F-actin and {beta}4, and explain why several other ABD-containing proteins that are expressed in basal keratinocytes are not recruited into hemidesmosomes.




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