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J. Biol. Chem., Vol. 279, Issue 21, 22773-22780, May 21, 2004

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Co-assembly of Envoplakin and Periplakin into Oligomers and Ca²⁺-dependent Vesicle Binding

IMPLICATIONS FOR CORNIFIED CELL ENVELOPE FORMATION IN STRATIFIED SQUAMOUS EPITHELIA^*

Andrey E. Kalinin, William W. Idler, Lyuben N. Marekov, Peter McPhie¶, Blair Bowers||, Peter M. Steinert, and Alasdair C. Steven**

From the Laboratory of Skin Biology and ^**Laboratory of Structural Biology, NIAMS, the ^¶Laboratory of Biochemistry and Genetics, NIDDK, and the ^||Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892

Plakin family members envoplakin and periplakin have been shown to be part of the cornified cell envelope in terminally differentiating stratified squamous epithelia. In the present study, purified recombinant human envoplakin and periplakin were used to investigate their properties and interactions. We found that envoplakin was insoluble at physiological conditions in vitro, and co-assembly with periplakin was required for its solubility. Envoplakin and periplakin formed soluble complexes with equimolar stoichiometry. Chemical cross-linking revealed that the major soluble form of all periplakin constructs and of envoplakin/periplakin rod domains was a dimer, although co-assembly of the full-length proteins resulted in formation of higher order oligomers. Electron microscopy of rotary-shadowed periplakin demonstrated thin flexible molecules with an average contour length of 88 nm for the rod-plus-tail fragment, and immunolabeling EM confirmed the molecule as a parallel, in-register, dimer. Both periplakin and envoplakin/periplakin oligomers were able to bind synthetic lipid vesicles whose composition mimicked the cytoplasmic side of the plasma membrane of eukaryotic cells. This binding was dependent on anionic phospholipids and Ca²⁺. These findings raise the possibility that envoplakin and periplakin bind to the plasma membrane upon elevation of intracellular [Ca²⁺] in differentiating keratinocytes, where they serve as a scaffold for cornified cell envelope assembly.

Received for publication, December 12, 2003 , and in revised form, March 3, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The paper is dedicated to the memory of Peter M. Steinert who passed away unexpectedly on April 7, 2003.

To whom correspondence should be addressed: Laboratory of Skin Biology, NIAMS, NIH, 9000 Rockville Pike, Bldg. 50, Rm. 1527, Bethesda, MD 20892-8023. Tel.: 301-496-7219; Fax: 301-402-3417; E-mail: kalinina{at}mail.nih.gov.

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