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Titolo:
Central role of the plakoglobin-binding domain for desmoglein 3 incorporation into desmosomes
Autore:
Andl, CD; Stanley, JR;
Indirizzi:
Univ Penn, Dept Dermatol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Dermatol, Philadelphia, PA 19104 USA
Titolo Testata:
JOURNAL OF INVESTIGATIVE DERMATOLOGY
fascicolo: 5, volume: 117, anno: 2001,
pagine: 1068 - 1074
SICI:
0022-202X(200111)117:5<1068:CROTPD>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CELL ADHESION; INTERMEDIATE FILAMENT ANCHORAGE; EPITHELIAL-CELLS; MEMBRANE CORE; CADHERINS; KERATINOCYTES; DESMOCOLLIN; JUNCTIONS; IDENTIFICATION; MOLECULES;
Keywords:
cadherin; desmosome assembly; plakoglobin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Stanley, JR Univ Penn, Dept Dermatol, 415 Curie Blvd,211 CRB, Philadelphia, PA 19104 USA Univ Penn 415 Curie Blvd,211 CRB Philadelphia PA USA 19104 USA
Citazione:
C.D. Andl e J.R. Stanley, "Central role of the plakoglobin-binding domain for desmoglein 3 incorporation into desmosomes", J INVES DER, 117(5), 2001, pp. 1068-1074

Abstract

The carboxy-termini of classical cadherins and desmocollins have been shown to play an important role in initiating desmosome assembly. In this studywe wanted to determine whether the carboxyterminal cytoplasmic domains of desmoglein 3 are important for targeting it to the desmosome. By generatingstably transfected A431 cell lines with chimeric constructs encoding for the extracellular domain of E-cadherin and the transmembrane and intracellular region of human desmoglein 3, we could show that the cytoplasmic tail issufficient to target the protein to the desmosome. By generating truncations of the carboxy-terminus we investigated the importance of the various intracellular subdomains. Whereas the construct encoding the intracellular cadherin-type segment domain still allowed its incorporation into the desmosome, further truncation, leaving only the intracellular anchor domain, did not. Deletion of the 87 amino acid long plakoglobin-binding site within the intracellular cadherin-type segment domain demonstrated that this region isessential for targeting desmoglein 3 to the desmosome. Absent the plakoglobin-binding site the chimeric molecule colocalizes with beta -catenin rather than desmoplakin. We conclude that binding of plakoglobin to desmoglein 3is an important step in desmosome assembly and leads to the incorporation of desmoglein 3 into the desmosome.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 23:36:46