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Titolo:
ASSOCIATION OF GAP-43 WITH DETERGENT-RESISTANT MEMBRANES REQUIRES 2 PALMITOYLATED CYSTEINE RESIDUES
Autore:
ARNI S; KEILBAUGH SA; OSTERMEYER AG; BROWN DA;
Indirizzi:
SUNY STONY BROOK,DEPT BIOCHEM & CELL BIOL STONY BROOK NY 11794 SUNY STONY BROOK,DEPT BIOCHEM & CELL BIOL STONY BROOK NY 11794
Titolo Testata:
The Journal of biological chemistry
fascicolo: 43, volume: 273, anno: 1998,
pagine: 28478 - 28485
SICI:
0021-9258(1998)273:43<28478:AOGWDM>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GPI-ANCHORED PROTEINS; KIDNEY EPITHELIAL-CELLS; NEURONAL GROWTH CONE; KINASE-C SUBSTRATE; TYROSINE KINASE; ALPHA-SUBUNIT; NEUROMODULIN GAP-43; SIGNAL-TRANSDUCTION; MDCK CELLS; T-CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
73
Recensione:
Indirizzi per estratti:
Citazione:
S. Arni et al., "ASSOCIATION OF GAP-43 WITH DETERGENT-RESISTANT MEMBRANES REQUIRES 2 PALMITOYLATED CYSTEINE RESIDUES", The Journal of biological chemistry, 273(43), 1998, pp. 28478-28485

Abstract

GAP-43 is an abundant protein in axonal growth cones of developing and regenerating neurons. We found that GAP-43 was enriched in detergent-resistant membranes (DRMs) isolated by Triton X-100 extraction from PC12 pheochromocytoma cells and could be detected in detergent-insoluble plasma membrane remnants after extraction of cells in situ, GAP-43 is palmitoylated at Cys-3 and Cys-4. Mutation of either Cys residue prevented association with DRMs. A hybrid protein containing the first 20amino acid residues of GAP-43 fused to beta-galactosidase was targeted to DRMs even more efficiently than GAP-43 itself. We conclude that tandem palmitoylated Cys residues can target GAP-43 to DRMs, defining anew signal for DRM targeting. We propose that tandem or closely spaced saturated fatty acyl chains partition into domains or ''rafts'' in the liquid-ordered phase, or a phase with similar properties, in cell membranes. These rafts are isolated as DRMs after detergent extraction. The brain-specific heterotrimeric G protein G(o), which may be regulated by GAP-43 in vitro, was also enriched in DRMs from PC12 cells, Targeting of GAP-43 to rafts may function to facilitate signaling throughG(o), In addition, raft association may aid in sorting of GAP-43 intoaxonally directed vesicles in the trans-Golgi network.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 09:30:28