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Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane
Address correspondence to F.M. Watt, Keratinocyte Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, UK. Tel.: 44 20 7269 3528. Fax: 44 20 7269 3078. email: fiona.watt{at}cancer.org.uk
Abstract
Periplakin forms part of the scaffold onto which the epidermal cornified envelope is assembled. The NH2-terminal 133 amino acids mediate association with the plasma membrane and bind a novel protein, kazrin. Kazrin is highly conserved and lacks homology to any known protein. There are four alternatively spliced transcripts, encoding three proteins with different NH2 termini. Kazrin is expressed in all layers of stratified squamous epithelia; it becomes membrane associated in the suprabasal layers, coincident with up-regulation of periplakin, and is incorporated into the cornified envelope of cultured keratinocytes. Kazrin colocalizes with periplakin and desmoplakin at desmosomes and with periplakin at the interdesmosomal plasma membrane, but its subcellular distribution is independent of periplakin. On transfection, all three kazrin isoforms have similar subcellular distributions. We conclude that kazrin is a novel component of desmosomes that associates with periplakin.
Key Words: epidermis; cornified envelope; microvilli; actin; differentiation
K. Nishi's present address is Frontier Research Laboratories, Pharmaceutical Research Division, Takeda Pharmaceutical Comapny Ltd., 10 Wadai, Tsukuba, Ibaraki 300-4293, Japan.
T. DiColandrea's present address is Corporate Research Biotechnology, Procter and Gamble, Miami Valley Labs, Cincinnati, OH 45252.
Abbreviations used in this paper: CE, cornified envelope; IF, intermediate filament.
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