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Titolo:
In vitro binding study of adaptor protein complex (AP-1) to lysosomal targeting motif (LI-motif)
Autore:
Fujita, H; Saeki, M; Yasunaga, K; Ueda, T; Imoto, T; Himeno, M;
Indirizzi:
Kyushu Univ, Fac Pharmaceut Sci, Div Physiol Chem, Fukuoka 8120054, Japan Kyushu Univ Fukuoka Japan 8120054 v Physiol Chem, Fukuoka 8120054, Japan Kyushu Univ, Fac Pharmaceut Sci, Div Immunobiochem, Fukuoka 8120054, JapanKyushu Univ Fukuoka Japan 8120054 Immunobiochem, Fukuoka 8120054, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 255, anno: 1999,
pagine: 54 - 58
SICI:
0006-291X(19990205)255:1<54:IVBSOA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBOXYL CYTOPLASMIC TAIL; ACID-PHOSPHATASE; MEMBRANE-PROTEIN; COATED VESICLES; INVITRO BINDING; SIALOGLYCOPROTEIN; CLATHRIN; ENDOCYTOSIS; RECEPTOR; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Himeno, M Kyushu Univ, Fac Pharmaceut Sci, Div Physiol Chem, Fukuoka 8120054, Japan Kyushu Univ Fukuoka Japan 8120054 Chem, Fukuoka 8120054, Japan
Citazione:
H. Fujita et al., "In vitro binding study of adaptor protein complex (AP-1) to lysosomal targeting motif (LI-motif)", BIOC BIOP R, 255(1), 1999, pp. 54-58

Abstract

Lysosomal membrane glycoproteins carry targeting information in cytoplasmic regions. Two distinct targeting motifs in these regions, GY (glycine-tyrosine) and LI (leucine-isoleucine), have been identified and characterized. Accumulating evidence suggests that the adaptor complexes (AP-1, AP-2, and AP-3) recognize this information in cytoplasmic tails of transmembrane proteins. Here we report two different in vitro analyses (affinity beads and surface plasmon resonance) which revealed specific interaction between the cytoplasmic tail of LGP85 and AP-1 but not so with AP-2. We also noted requirement of the LI motif of the LGP85 tail in binding to the AP-1 complex. Ourdata and others which indicated the binding of AP-3 to the LIMP II (synonym of LGP85) tail suggest that the cytoplasmic tail of LGP85 interacts with AP-1 at the trans-Golgi network (TGN) and AP-3 at late endosomes, respectively. We propose that this sequential interaction between the lysosomal targeting signal and distinct APs along its transport pathway is responsible for the critical sorting of lysosomal membrane proteins and/or the potential proofreading system of mistargeted molecules. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 01:13:46