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Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane

Periplakin forms part of the scaffold onto which the epidermal cornified envelope is assembled. The NH(2)-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 alterna...

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Detalles Bibliográficos
Autores principales: Groot, Karen R., Sevilla, Lisa M., Nishi, Kazunori, DiColandrea, Teresa, Watt, Fiona M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172441/
https://www.ncbi.nlm.nih.gov/pubmed/15337775
http://dx.doi.org/10.1083/jcb.200312123
Descripción
Sumario:Periplakin forms part of the scaffold onto which the epidermal cornified envelope is assembled. The NH(2)-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 NH(2) 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.