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Titolo:
Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation
Autore:
Okazaki, N; Yan, J; Yuasa, S; Ueno, T; Kominami, E; Masuho, Y; Koga, H; Muramatsu, M;
Indirizzi:
Helix Res Inst, Chiba 2920812, Japan Helix Res Inst Chiba Japan 2920812Helix Res Inst, Chiba 2920812, Japan Chiba Univ, Sch Med, Dept Anat & Dev Biol, Cyuo Ku, Chiba 2608670, Japan Chiba Univ Chiba Japan 2608670 & Dev Biol, Cyuo Ku, Chiba 2608670, Japan Juntendo Univ, Sch Med, Dept Biochem, Bunkyo Ku, Tokyo 1138421, Japan Juntendo Univ Tokyo Japan 1138421 ochem, Bunkyo Ku, Tokyo 1138421, Japan
Titolo Testata:
MOLECULAR BRAIN RESEARCH
fascicolo: 1-2, volume: 85, anno: 2000,
pagine: 1 - 12
SICI:
0169-328X(200012)85:1-2<1:IOTUKA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
CAENORHABDITIS-ELEGANS; RAT-LIVER; SERINE/THREONINE KINASE; ENDOPLASMIC-RETICULUM; AUTOPHAGIC VACUOLE; GABA(A) RECEPTORS; VESICLE FUSION; C-ELEGANS; MEMBRANES; YEAST;
Keywords:
UNC-51 protein kinase; GABARAP; GATE-16; axonal elongation; vesicular transport; autophagy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Okazaki, N Helix Res Inst, 1532-3 Yana, Chiba 2920812, Japan Helix Res Inst 1532-3 Yana Chiba Japan 2920812 2920812, Japan
Citazione:
N. Okazaki et al., "Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation", MOL BRAIN R, 85(1-2), 2000, pp. 1-12

Abstract

We identified two mammalian ULK1 (Unc-51-like kinase involved in neurite extension) binding proteins by yeast two-hybrid screening. Both proteins showed high structural similarity to microtubule-associated protein (MAP) Light chain 3 (LC3). One is identical to the Golgi-associated ATPase Enhancer of 16 kDa (GATE-16), an essential factor for intra-Golgi transport [39]. Theother is identical to the gamma 2-subunit of GABA-A receptor associated protein (GABARAP) which has a possible role in receptor transport [46]. Usingthe yeast two-hybrid system and the in vitro GST pull-down assay, we foundthat the N-terminal proline/serine rich (PS) domain of ULK1 (amino acid 287-416) is required for ULK1-GATE-16 and ULK1-GABARAP protein interactions. However, the kinase activity of ULK1 affected neither ULK1-GATE-16 nor ULK1-GABARAP interaction. Immunohistochemical analysis using ULK1 and GABARAP antibodies showed that the ULK1 and the GABARAP proteins co-localized to many kind of neurons such as pyramidal cells of the hippocampus, mitral cells of the olfactory bulb, and Purkinje cells of the cerebellum. In HeLa cells,endogenous ULK1 and tagged GABARAP showed punctate structures in the cytosol, and were colocalized. These results suggest that the interaction of ULK1 and GABARAP is important to vesicle transport and axonal elongation in mammalian neurons. (C) 2000 Elsevier Science BN. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:08:01